Title of Invention

ALKALINE MANNANASES FROM BACILLUS SP

Abstract

The present invention relates to an isolated mannanase, which is (a) A polypeptide encodable by the mannanase enzyme encoding part of the DNA sequence cloned into the plasmid present in Escherichia coli DSM 12441, or (b) A polypeptide comprising an amino acid sequence as shown in positions 31-330 of SEQIDNO: 12,or (c) A polypeptide encodable by the DNA sequence as shown in positions 97-993 of SEQIDNO:ll,or (d) An analogue of the polypeptide defined in (a) or (b) which is at least 85% homologous with said polypeptide, or a fragment of (a), (b) or (c).

Full Text

NOVEL MANNANASES The present invention relates to -microbial mannanases, more specifically to microbial enzymes exhibiting mannanase activity as their major enzymatic activity in the neutral and alkaline pH ranges; to a method of producing such enzymes; and to methods for using such enzymes in the paper and pulp, textile, oil drilling, cleaning, laundering, detergent and cellulose fiber processing industries. BACKGROUND OF THE INVENTION Mannan containing polysaccharides are a major component of hues hemicellulose fraction in woods and endosperm in many leguminous seeds and in some mature seeds of non-legurrdnous plants. Essentially unsubstituted linear beta-1,4-mannan is found in some non-leguminous plants, Unsubstituted beta-1,4-mannan which is present e.g. in ivory nuts resembles cellulose in the conformation of she individual polysaccharide chains, and is water-insoluble. In leg ominous seeds, water-soluble galactomannan is the main storage carbohydrate comprising up to 20% of the total dry weight. Galactomannans have a linear beta-1,4-mannan backbone substituted with single alpha-1,6-galactose, optionally substituted with acetyl groups. Mannans are also found in several monocotyledonous-..plants the most abundant polysaccharides in the cell wall material in palm. kernel meal. Gluccmannans are linear polysaccharides with a backbone of beta-1,4-linked mannose and glucose alternating in a more or less regular manner, he backbone optionally being substituted with galactose and/or acetyl groups. Hanna’s, galactomannans, gluccmannans and gHilactcglc.cG:T.£nnans (i.e. glucomannan backbones with branched galactose) contribute to more than 50% of the softwood hemicellulose. Moreover, the cellulose of many red algae contains a significant amount of mannose. Mannanases have been identified in several Bacillus organisms. For example, Talbot et al., Appl. Environ. Microbiol., Vol.56, No. II, pp. 3505-3510 (1990) describes a beta-mannanase derived from Bacillus stearothermophilus in dimer form having molecular weight of 162 kDa and an optimum pH of 5.5-7.5. Mendoza et al., World J. Microbial. Biotech., Vol. 10, No. 5, pp. 551-555 (1994) describes a beta-mannanase derived from Bacillus subtitles having a molecular weight of 38 kDa, an optimum activity at pH 5.0 and 55^C and a pi of 4.8. JP-A-03047076 discloses a beta-mannanase derived from Bacillus sp. r having a molecular weight of 37±3 kDa measured by gel filtration, an optimum pH of, 8-10 and a pi of 5.3-5.4. JP-A-63055289 describes the production of an alkaline, thermostable beta-mannanase which hydrolyses beta-1, 4-D-mannopyranoside bonds of e.g. mannans and produces manno-oligosaccharides. JP-A-63036775 relates to the Bacillus microorganism FERM P-8856 which produces beta-mannanase and beta-mannosidase at an alkaline pH. JP-A-08051975 discloses alkaline beta-mannanases from alkalophilic Bacillus sp. AM-001 having molecular weights of 43±3 kDa and 57±3 kDa and optimum pH of 8-10. A purified mannanase from Bacillus amyloliquefaciens useful in the bleaching of pulp and paper and a method of preparation thereof is disclosed in WO 97/11164. WO 91/18974 describes a hemicellulase such as a glutamate, xylanase or mannanase active at an extreme pH and temperature. WO 94/2557 6 discloses an enzyme from Aspergillums aculeate, CBS 101.43, exhibiting mannanase activity which may be useful for degradation or modification of plant or algae cell wall material. WO 93/24622 discloses a mannanase isolated from Trichoderma reseed useful for bleaching lignocelluloses pulps. WO 95/35362 discloses cleaning compositions containing - -plant cell wall degrading enzymes having peptidase and/or hemicellulase and optionally cellulase activity for the removal of stains of vegetable origin and further discloses an alkaline mannanase from the strain C11SB.G17. It is an object of the present invention to provide a novel 1 and efficient enzyme exhibiting mannanase activity also in the Alkaline pH range, e.g. when applied in cleaning compositions or different industrial processes. SUMMARY OF THE INVENTION The inventors have now found novel enzymes having substantial mannanase activity, i.e. enzymes exhibiting mannanase activity which may be obtained from a bacterial strain of the genus Bacillus and have succeeded in identifying DNA sequences encoding such enzymes. The DNA sequences are listed in the sequence listing as SEQ ID No. 1, 5, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29 and 31; and the deduced amino acid sequences are listed in the sequence listing as SEQ ID No. 2, 6, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30 and 32, respectively. It is believed that the novel enzymes will be classified according to the Enzyme Nomenclature in the Enzyme Class EC 3.2.1.78. In a first aspect, the present invention relates to a mannanase which is i) a polypeptide produced by Bacillus sp. 1633, ii) a polypeptide comprising an amino acid sequence as shown in positions 31-330 of SEQ ID N0:2, or iii) an analogue of the polypeptide defined in i) or ii) which is at least 65% homologous with said polypeptide, is derived from said polypeptide by substitution, deletion or addition of one or several amino acids, or is immunological reactive with a polyclonal antibody raised against said polypeptide in purified form. Within one aspect, the present invention provides an isolated polynucleotide molecule selected from the group consisting of (a) polynucleotide molecules encoding a polypeptide having mannanase activity and comprising a sequence of nucleotides as shown in SEQ ID NO: 1 from nucleotide 91 to nucleotide 990; (b) species homology of (a); (c) polynucleotide molecules that encode a polypeptide having mannanase activity that is at least 65% identical to the amino acid sequence of SEQ ID NO: 2 from amino acid residue 31 to amino acid residue 330; (d) molecules complementary to (a), (b) or (c); and (e) degenerate nucleotide sequences of (a), (b), (c) or (d). The plasmid pBXM3 comprising the polynucleotide molecule (the DNA sequence) encoding a mannanase of the present invention has been transformed into a strain of the Escherichia coli which was deposited by the inventors according to the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Sampling von Mikroorganismen und Zellkulturen GmbH, Masquerader Weg lb, D-3812 4 Braunschweig, Federal Republic of Germany, on 29 May 1998 under the deposition number DSM 12197. Within another aspect of the invention there is provided an expression vector comprising the following operably linked elements: a transcription promoter; a DNA segment selected from the group consisting of (a) polynucleotide molecules encoding a polypeptide having mannanase activity and comprising a sequence of nucleotides as shown in SEQ ID NO: 1 from nucleotide 91 to nucleotide 990; (b) species homologs of (a); {c) polynucleotide molecules that encode a polypeptide having mannanase activity that is at least 65% identical to the amino acid sequence of SEQ ID NO: 2 from amino acid residue 31 to amino acid residue 330; and (d).degenerate nucleotide sequences of (a), (b), or (c); and a transcription terminator. .. . Within yet another aspect of. the„-present invention there is provided a cultured cell into which has been introduced an expression vector as disclosed above, wherein said cell expresses the polypeptide encoded by the DNA segment. Further aspects of the present invention provide an isolated polypeptide having mannanase activity selected from the group consisting of* (a) polypeptide molecules comprising a sequence of amino acid residues as shown in SEQ ID NO:2 from amino acid residue 31 to amino acid residue 330; (b) species homologs of (a); and a fusion protein having mannanase activity comprising a first polypeptide part exhibiting mannanase activity and a second polypeptide part exhibiting cellulose binding function, the second polypeptide preferably being a cellulose binding domain (CBD), such as a fusion protein represented by SEQ ID NO:4. Within another aspect of the present invention there is provided a composition comprising a purified polypeptide according to the invention in combination with other polypeptides. Within another aspect of the present invention there are provided methods for producing a polypeptide according to the invention comprising culturing a cell into which has been introduced an expression vector as disclosed above, whereby said cell expresses a polypeptide encoded by the DNA segment and recovering the polypeptide. The novel enzyme of the present invention is useful for the treatment of cellulosic material, especially cellulose-containing fiber, yarn, woven or non-woven fabric, treatment of mechanical paper-making pulps, Kraft pulps or recycled waste paper, and for retting of fibres. The treatment can be carried out during the processing of cellulosic material into a material ready for manufacture of paper or of garment or fabric, the latter e.g. in the desizing or scouring step; or during industrial or household laundering of such fabric or garment. Accordingly, in further aspects the present invention relates to a cleaning or detergent composition comprising the enzyme of the invention; and to use of the enzyme of the invention -for the--treatment, eg . cleaning,~.o± .cellulose-containing fibers, yarn, woven or non-woven fabric, as well as synthetic or partly synthetic fabric. It is contemplated that the enzyme of the invention is useful in aria enzymatic scouring process and/or desizing (removal of mannan size) in the preparation of cellulosic material e.g. for proper response in subsequent dyeing operations. Tiled enzyme is also useful for removal of mannan containing print paste. Further, detergent compositions comprising the novel enzyme are capable of removing or bleaching certain soils or stains present on laundry, especially soils and spots resulting from mannan containing food, plants, and the like. Further, treatment with cleaning or detergent compositions comprising the novel enzyme can improve whiteness as well as prevent binding of certain soils to the cellulosic material. Accordingly, the present invention also relates to cleaning compositions, including laundry, dishwashing, hard surface cleaner, personal cleansing and oral/dental compositions, comprising the mannanase of the- invention. Further, the present invention relates to such cleaning compositions comprising a mannanase and an enzyme selected from cellulases, proteases, lipases, amylases, pectin degrading enzymes and xyloglucanases, such compositions providing superior cleaning performance, i.e. superior stain removal, dingy cleaning or whiteness maintenance . DEFINITIONS Prior to discussing this invention in further detail, the following terms will first be defined. The term "orthodox" (or homolog') denotes a polypeptide or protein obtained from one species that has homology to an analogous polypeptide or protein from a different species. The term prolog" denotes a polypeptide or protein obtained from a given species that has homology to a distinct polypeptide or protein from that same species. The term "expression vector" denotes a DNA molecule, linear or circular, that comprises a segment encoding~a polypeptide of interest operably linked to additional segments that provide for its transcription. Such additional segments may include promoter and terminator sequences, and may optionally include one or more origins of replication, one or more selectable markers, an enhancer, a polyadenylation signal, and the like. Expression vectors are generally derived from 'plasmid or viral DNA, or may contain elements of burgh. The expression vector of the invention may be any expression vector that is conveniently subjected to recombinant DNA procedures, and the choice of vector will often depend on the host cell into which the vector is to be introduced. Thus, the vector may be an autonomously replicating vector, i.e. a vector which exists as an extrachromosomal entity, the replication of which is independent of chromosomal replication, e.g. a plasmid. Alternatively, the vector may be one which, when introduced into a host cell, is integrated into the host cell genome and replicated together with the chromosome(s) into which it has been integrated. The term ^"^recombinant expressed" or "recombinant expressed" used herein in connection with expression of a polypeptide or protein is defined according to the standard definition in the art. Recombinantly expression of a protein is generally performed by using an expression vector as described immediately above. The term "isolated", when applied to a polynucleotide molecule, denotes that the polynucleotide has been removed from its natural genetic milieu and is thus free of other extraneous or unwanted coding sequences, and is in a form suitable for use within genetically engineered protein production systems. Such isolated molecules are those that are separated from their natural environment and include cDNA and genomic clones. Isolated DMA molecules of the present invention are free of other genes with which they are ordinarily associated, but may include naturally occurring 5* and 3* untranslated regions such as promoters and terminators. The identification of associated regions will be evident to one of ordinary skill in the art (see for example, Dyne and Texan, Nature -316:-7- Z8,- 1985) ■ The term "'an isolated polynucleotide" may alternatively be termed "'a cloned polynucleotide". When applied to a protein/polypeptide, the term "isolated" indicates that the protein is found in a condition other than its native environment. In a preferred form, the isolated protein is-substantially free of other proteins, particularly other homologous proteins (i.e. "homologous impurities" (see below)). It is preferred to provide the protein in a greater than 40% pure form, more preferably greater than 60% pure form. Even more preferably it is preferred to provide the protein in a highly purified form, i.e., greater than 80% pure, more preferably greater than 95% pure, and even more preferably greater than 99% pure, as determined by SDS-PAGE. The term isolated protein/polypeptide may alternatively be termed 'purified protein/polypeptide". The term "homologous impurities" means any impurity (e.g. another polypeptide than the polypeptide of the invention) which originate from the homologous cell where the polypeptide of the invention is originally obtained from. The term "obtained from" as used herein in connection with a specific microbial source, means that the polynucleotide and/or polypeptide is produced by the specific source (homologous expression), or by a cult in which a gene from the source have been inserted (heterologous expression]. The term "operably linked", when referring to DNA segments, denotes that the segments are arranged so that they function in concert for their intended purposes, e.g. transcription initiates in the promoter and proceeds through the coding segment to the terminator The term "polynucleotide" denotes a single- or double- stranded polymer of deoxyribonucleotide or rib nucleotide bases read from the 5* to the 3' end. Polynucleotides include RNA and DNA, and may be isolated from natural sources, synthesized in victor or prepared from a combination of natural and synthetic molecules. _ ,_ The term "complements of polynucleotide molecules" denotes polynucleotide molecules having a complementary base sequence and reverse orientation as .compared to a reference sequence. For example, the sequence 5' ATGGACGGG 3' is complementary to 5' CCCGTGCAT 3'. The term "degenerate nucleotide sequence" denotes a sequence of nucleotides that includes one or more degenerate codons (as compared to a reference polynucleotide molecule that encodes a polypeptide). Degenerate codons contain different triplets of nucleotides, but encode the same amino acid residue (i.e., GAU and GAG triplets each encode Asp). The teen "promoter" denotes a portion of a gene containing DNA sequences that provide for the binding of RNA polymerase and initiation of transcription. Promoter sequences are commonly, but not always, found in the 5' non-coding regions of genes. The term "secretory signal sequence" denotes a DNA sequence that encodes a polypeptide (a "secretory peptide") that, as a component of a larger polypeptide, directs the larger polypeptide through a secretory pathway of a cell in which it is synthesized. The larger peptide is commonly cleaved to remove the secretory peptide during transit through the secretory pathway. The term "enzyme core" denotes a single domain enzyme which may or may not have been modified or altered, but which has retained its original activity; the catalytic domain as known in the art has remained intact and functional. By the term 'linker" or "spacer" is meant a polypeptide comprising at least two amino acids which may be present between the domains of a multinomial protein, for example an enzyme comprising an enzyme core and a binding domain such as a cellulose binding domain (CBD) or any other enzyme hybrid, or between two proteins or polypeptides expressed as a fusion polypeptide, for example a fusion protein comprising two core enzymes. For example, the fusion protein of an enzyme core with a CBD is provided by fusing a DNA sequence encoding the enzyme core, a DNA sequence encoding the linker and a DNA sequence encoding the CBD sequentially into one open reading frame and expressing this construct. The term "mannanase" or "galactomannanase" denotes a man-nanas enzyme defined according to the art as officially being named mannan endo-1,4-beta-mannosidase and having the alternative names-" beta-madman’s and endo-1, 4-mannanase and catalyst-g ■ hydrolyses of 1,4-beta-D-mannosidic linkages in mannans, gaiac-tomannans, glucomannans, and galactoglucomannans which enzyme is classified according to the Enzyme Nomenclature as EC 3.2.1.78 (http://www.expasy,ch/enzyme). DETAILED DESCRIPTION OF THE INVENTION HOW TO USE A SEQUENCE OF THE INVENTION TO GET OTHER RELATED SEQUENCES: The disclosed sequence information herein relating to a polynucleotide sequence encoding a mannanase of the invention can be used as a tool to identify other homologous mannanases. For instance, polymerase chain reaction (PCR) can be used to amplify sequences encoding other homologous mannanases from a variety of microbial sources, in particular of different Eacii-lus species. ASSAY FOR ACTIVITY TEST A polypeptide of the invention having mannanase activity may be tested for mannanase activity according to standard test procedures known in the art, such as by applying a solution to be tested to 4 mm diameter holes punched out in agar plates containing 0.2% AZCL galactomannan (carob), i.e. substrate for the assay of endo-1,4-beta-D-mannanase available as CatNo.I-AZGMA forcer; the company Magazine (Magazine’s Internet address: hertz: //www.megazyme-coTTi/Purchase/index.html) . POLYNUCLEOTIDES Within preferred embodiments of the invention an isolated polynucleotide of the invention will hybridize to similar sized. regions of SEQ ID NO: 1, or a sequence complementary thereto, under at least medium stringency conditions. In particular polynucleotides of the invention will hybridize to a denatured double-stranded DNA probe comprising either the full sequence shown in SEQ ID N0:1 or a partial sequence comprising the segment shown in positions 91-990 of SEQ ID N0:1 which segment encodes for the catalytically active domain or enzyme' core of the manganese-oi the invention or any probe comprising a subsequence shown in positions 91-990 of SEQ ID N0:1 which subsequence has a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in derail below. Suitable experimental conditions for determining hybridization at medias, or high stringency between a nucleotide probe and a homologous DNA or RNA sequence involves' firesoaking of the filter containing the DNA fragments or RNA to hybridize in 5 X SSC (Sodium chloride/Sodium citrate, Sambrook et al. 1989) for 10 min, and prehybridization of the filter in a solution of 5 X SSC, 5 x Reinhardt’s solution (Sambrook et al. 1989), 0.5 % SDS and 100 ]yo/ml of denatured solicited salmon sperm DNA (Sambrook et al. 1989), followed by hybridization in the same solution containing a concentration of long/ml of a random-primed (Feinberg, A. P. and Vogelstein, E. (1983) Anal. Biochem. 132:6-13), 32P-dCTP-labeled (specific activity higher than 1 X 10 cam/ g) probe for 12 hours at ca. 45°C. The filter is then washed twice for 30 minutes in 2 x SSC, 0.5 % SDS at least 60°C (medium stringency), still more preferably at least 65°C (medium/high stringency), even more preferably at least 70°C (high stringency), and even more preferably at least 75°C (very high stringency). Molecules to which the oligonucleotides probe hybridizes under these conditions are detected using a x-ray film. Other useful isolated polynucleotides are those which will hybridize to similar sized regions of SEQ ID NO: 5, SEQ ID NO: 9, SEQ ID NO: 11, SEQ ID NO: 13, SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 19, SEQ ID NO: 21, SEQ ID NO: 23, SEQ ID NO: 25, SEQ ID NO: 27, SEQ ID NO: 29 or SEQ ID NO: 31, respectively, or a sequence complementary thereto, under at least medium .stringency ' conditions. Particularly useful are polynucleotides which will hybridize to a denatured double-stranded DNA probe comprising either the full sequence shown in SEQ ID NO:5 or a partial sequence comprising the segment shown in positions 94-1032 of SEQ ID NO:5 i which segment-^encodes for the catalytically active domain or enzyme core "cN the mannanase of the invention or any probe comprising a subsequence shown in positions 94-1032 of SEQ ID NO:5 which subsequence has a length of at least about 100 base pairs under at least midair. stringency conditions, but '. preferably at high stringency conditions as described in detail above; as well as polynucleotides which will hybridize to a denatured double-stranded DNA probe comprising either the full sequence shown in SEQ ID NO:9 or a partial sequence comprising the segment shown in positions 94-1086 of SEQ ID NO:9 which segment encodes for the catalytically active domain or enzyme core of the mannanase of the invention or any probe comprising a subsequence shown in positions 94-1086 of SEQ ID NO:9 which subsequence has a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in detail above; as well as polynucleotides which will hybridize to a denatured double-stranded DNA probe comprising either the full sequence shown in SEQ ID NO:11 or a partial sequence comprising the segment shown in positions 97-993 of SEQ ID NO:11 which segment encodes for the catalytically active domain or enzyme core of the mannanase of the invention or any probe comprising a subsequence shown in positions 97-993 of SEQ ID NO:11 which subsequence has a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in detail above; as well as polynucleotides which will hybridize to a denatured double-stranded DNA probe comprising either the full sequence shown in SEQ ID NO:13 or a partial sequence comprising the segment shown in positions 498-1464 of SEQ ID NO:13 which segment encodes for the catalytically active domain or enzyme core, of the mannanase of the invention or any probe comprising a subsequence shown in positions 498-1464 of SEQ ID NO:13 which subsequence has a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in detail above; as well as 'polynucleotides which will hybridize to a denatured double-stranded DNA probe comprising either the full sequence shown in SEQ ID NO:15 or a partial sequence comprising the segment shown in positions -204-1107 of SEQ ID NO:15 which segment encodes for the catalytically active domain or enzyme core of the mannanase ) of the invention or any probe comprising a subsequence shown in Positions 204-1107 of SEQ ID NO:15 which subseauence has a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in detail above; as well as polynucleotides which will hybridize to a denatured double-stranded DNA probe comprising either the sequence shown in SEQ ID NO:17 or any probe comprising a subsequence of SEQ ID NO:17 which subsequence has a length of at least about 100 base oars under at least medium stringency conditions, but preferably at high stringency conditions as described in detail above; as well as polvTiucleotides which will hybridize to a denatured double-stranded DNA probe comprising either the sequence shown in SEQ ID NO:19 or any probe comprising a subsequence of SEQ ID NO:19 which subsequence has a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in detail above; as well as polynucleotides which will hybridize to a denatured double-stranded DNA probe comprising either the full sequence shown, in SEQ IC NO:21 or a partial sequence comprising the segment shown in positions 38-960 of SEQ ID N0:21 which segment encodes for the catalytically active domain or enzyme core of rhe mannanase of the invention or any probe comprising a subsequence shown in positions 88-950 of SEQ ID NO:21 which subsequence has a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency . conditions as described in detail above; as well as polynucleotides which will hybridize to a denatured double-stranded DNA probe comprising either the full sequence shown in SEQ ID NO:23 or any probe comprising a subsequence of SEQ ID NO:23 which subsequence has a length of at least about 100 base pairs under at least media’s stringency conditions, but preferably at high stringency conditions as described in detail above; as well as polynucleotides which will hybridize to a denatured double-stranded DNA probe comprising either the full sequence shown in SEQ ID NO:25 or a partial sequence comprising the segment shown in positions 904-1874 of SEQ ID NO:25 which segment encodes for the catalytically active domain or enzyme core of the mannanase of the invention or any probe comprising a subsequence shown in positions 904-1874 of SEQ ID 1SI0:25 which subsequence has a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in detail above; as well as polynucleotides which will hybridize to a denatured double-stranded DNA probe comprising either the full sequence shown in SEQ ID NO:27 or a partial sequence comprising the segment shown in positions 4.98-1488 of SEQ ID NO:27-which segment encodes for the catalytically active domain or enzyme core of the mannanase of the invention or any probe comprising a subsequence shown in positions 498-1488 of SEQ ID NO:27 which subsequence has a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in detail above; as well as polynucleotides which will hybridize to a denatured double-stranded DNA probe comprising either the full sequence shown in SEQ ID NO:29 or a partial sequence comprising the segment shown in positions 79-1083 of SEQ ID NO:29 which segment encodes for -the catalytically active domain or enzyme core of the mannanase of the invention or any probe comprising a subsequence shown in positions 79-1083 of SEQ ID NO:29 which subsequence has a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in detail above; as well as polynucleotides which will hybridize to a denatured double-stranded DNA probe comprising either. the full sequence shown in SEQ ID NO:31 or a partial sequence comprising the segment shown in positions 1779-2709 of SEQ ID NO:31 which segment encodes for the" ca"tai-ytically active dome-in or enzyme core of the-mannanase' of the invention or any probe comprising a subsequence shown in positions 1779-2709 of SEQ ID NO:31 which subsequence has a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in detail above. As previously noted, the isolated polynucleotides of the present invention include DNA and RNA. Methods for isolating DNA and RNA are well known in the art. DNA and RNA encoding genes of interest can be cloned in Gene Banks or DNA libraries by means of methods known in the art. Polynucleotides encoding polypeptides having mannanase activity of the invention are then identified and isolated by, for example, hybridization or PCR. The present invention further provides counterpart polypeptides and polynucleotides from different bacterial strains (orthodox or paralogs). Of particular interest are mannanase polypeptides from gram-positive alkalophilic strains, including species of Bacillus such as Bacillus sp., Bacillus agaradhaerens, Bacillus halodurans, Bacillus clause and Bacillus licheniformis7 and mannanase polypeptides from Thermoanaerohacter group, including species of CaldicellulosiruptoT. Also mannanase polypeptides from the fungus Benicia or Scytalidium, in particular the species Hum cola inclines or thermophilumr £-e of interest. Species homologues of a polypeptide with iriannanase activity of the invention can be cloned using information and compositions provided by the present invention in combination with conventional cloning techniques. For example, a DNA sequence of the present invention can be cloned using chromosomal DNA obtained from a cell type that expresses the protein. Suitable sources of DNA can be identified by probing Northern or Southern blots with probes designed from the sequences disc-loosed herein. A library is then prepared from •chromosomal DNA of a positive cell line. A DNA sequence of the invention encoding an- polypeptide having mannanase activity can then be isolated by a variety oY'metlTods, such as by probing with probes designed from -the sequences disclosed in the present specification and claims or with one or more sets of degenerate probes based on the disclosed sequences. A DNA sequence of the invention can also be cloned using the polymerase chain reaction, or PCR {Mullis, U.S. Patent 4,683,202), using primers designed from the sequences disclosed herein. Within an additional method, the DNA library can be used to transform or transfected host cells, and expression of the DNA of interest can be detected with an antibody (mono-clonal or polyclonal) raised against the mannanase cloned from M.p, expressed and purified as described in Materials and Methods and Example 1, or by an activity test relating to a polypeptide having mannanase activity. The mannanase encoding part of the DNA sequence (SEQ ID N0:1) cloned into plasmid pBXM3 present in Escherichia coli DSM 12197 and/or an analogue DNA sequence of the invention may be cloned from a strain of the bacterial species Bacillus sp. 1633, or another or related organism as described herein. The mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:5) was transformed a strain of the Escherichia coli which was deposited by the inventors according to the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Sainmlung von Mikroorganismen ulna Zellkulturen Gerbil, Masquerader Weal lb, D-36124 Braunschweig, Federal Republic of GerxTLany, on 18 May 1998 under the deposition number DSM 12180; this mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:5) and/or an analogue DNA sequence thereof may be cloned from a strain of the bacterial species 'Bacchius agaradhaerens, for example from the type strain DSM 8721, or another or related organism as described herein. The mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:9) was transformed a strain of the Escherichia coli which was deposited by the inventors according' to the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Samsung von Mikroorganismen und Zellkulturen GmbH, Masquerader Weg lb, D-38124 Braunschweig, Federal Republic of Germany, on 7 October 1998 under the deposition number DSM 12433; this mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:9) and/or an analogue DNA sequence thereof may be cloned from a strain of the bacterial species Bacillus sp. AAI12 or another or related organism as described herein. The mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:11) was transformed a strain of the Escherichia coli which was deposited by the inventors according to the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Samsung von Mikroorganismen und Zellkulturen GmbH, Masquerader Weg lb, D-38124 Braunschweig, Federal Republic of Germany, on 9 October 1998 under the deposition number DSM 12441; this mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:11) and/or an analogue DNA sequence thereof may be cloned from a strain of the bacterial species Bacillus halodurans or another or related organism as described herein. The mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:13) was transformed a strain of the Escherichia coli which was deposited by the inventors according to the Budapest Treaty on the International Precognitions of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Samsung von Mikroorganismen und Zellkulturen GmbH, Masquerader Weg lb, D-38124 Braunschweig, Federal Republic of Germany, on 11 May 1995 under the deposition number DSM 9 98 4; this mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO: 13.) and/or an analogue DNA sequence thereof may be cloned from a strain of the fungal species Hum cola insolents or another or related organism as described herein. The mannanase encoding part of'the"poiyhucleotide molecule (the DNA sequence of SEQ ID NO: 1-5-} was transformed a strain of the Escherichia coli which was deposited by the inventors according to the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Samsungs von Mikroorganismen und Zellkulturen GmbH, Masquerader Weg lb, D-38124 Braunschweig, Federal Republic of Germany, on 5 October 1998 under the deposition number DSM 12432; this mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:15) and/or an analogue- DNA sequence thereof may be cloned from a strain of the bacterial species Bacillus sp. AA349 or another or related organism as described herein. The mannanase encoding part of the polynucleotide molecule (rhe DNA sequence of SEQ ID NO:17) was transformed a strain of he Escherichia cull which was deposited by the inventors according to the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg lb, D-38124 Braunschweig, Federal Republic of Germany, on 4 June 1999 under the deposition number DSM 12847; this mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:17) and/or an analogue DNA sequence thereof may be cloned from, a strain of the bacterial species Bacillus sp. or anorher cur related organism as described herein. The mannanase -encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:19) was transformed a strain of the Escherichia coll which was deposited by the inventors according to the Budapest Treaty on the International Recognition'Of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg lb, D-38124 Braunschweig, Federal Republic of Germany, on 4 June 19 99 under the deposition number DSM 12848; this mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:19) and/or an analogue DNA sequence thereof may be cloned from a strain of-the bacterial species Bacillus sp. or another or related organism as described herein. The mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:21) was transformed a strain of the Escherichia coll which was deposited by the inventors according to the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg lb, D-38124 Braunschweig, Federal Republic of Germany, on 4 June 1999 under the deposition number DSM 12849; this mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:21) and/or an analogue DNA sequence thereof may be cloned from a strain of the bacterial species Bacillus clause or another or related organism as described herein. The mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:23) was transformed a strain of the Escherichia coli which was deposited by the inventors according to the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg lb, D-38124 Braunschweig, Federal Republic of Germany, on 4 June 1999 under the deposition number Simi 12850; this manganese encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:2 3) and/or an analogue DNA sequence thereof may be cloned from a strain of the bacterial species Bacillus sp. or another or related organism as described herein. The mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:25) was transformed a strain of the Escherichia coli which was deposited by the inventors according to the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg lb, D-38124 Braunschweig, Federal Republic of Germany, on 4 June 1999 under the deposition number DSM 12846; this mannanase encoding part of the polynucleotide molecule (the DNA, sequence of SEQ ID NO: 25) and/or an analogue DNA sequence thereof may be cloned from a strain of the bacterial species Bacillus sp. or another, or related organism as described herein. The mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO: 27) was transformed a strain of the Escherichia coli which was deposited by the inventors according to the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Sampling von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg lb, D-38124 Braunschweig, Federal Republic of Germany, on 4 June 1999 under the deposition number DSM 128 51; this mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:27) and/or an analogue DNA sequence thereof may be cloned from a strain of the bacterial species Bacillus sp. or another or related organism as described herein. —J The mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:29) was transformed a strain of the Escherichia coli which was deposited by the inventors according to the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg lb, D-38124 Braunschweig., Federal Republic of Germany, on 4 June 1999 under the deposition number DSM 12852; this mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:29) . , and/or an analogue DNA sequence thereof may be cloned from a strain of the bacterial species Bacillus licheniformis or another or related organism as described herein. The mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:31) was transformed a strain of the Escherichia coli which was deposited by the inventors ■ according to the Budapest Treaty on the International Recognition of the Deposer of Microorganisms for the Purposes of Patent Procedure at the Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg lb, D-38124 Braunschweig, Federal Republic of Germ. any, on 5 October 1998 under the deposition number DSM 12435; this mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:31) and/or an analogue DNA sequence thereof may be cloned from a strain of the bacterial species Caldicellulosiruptor sp. or another or related organism as described herein. Alternatively, the analogous sequence may be constructed on ■chew basis of the DNA sequence obtainable from the plasmid present in Escherichia coll DSM 12197 (which is believed to be identical to the attached SEQ ID N0:1), the plasmid present in Escherichia coli DSM 12180 (which is believed to be identical to rhe attached SEQ ID N0:5), the plasmid present in Escherichia coll DSM 12433 (which is believed to be identical to the attached SEQ ID N0:9), the plasmid present in Escherichia coll DSM 12441 (which is believed to be identical to the attached SEQ ID N0:11), the plasmid present in Escherichia coli DSM 9984 (which is believed to be identical to the attached SEQ ID N0:13)^ the plasmid present in Escherichia coli DSM 12432 (which is believed to be identical to the attached SEQ ID NO:15), the plasmid present in Escherichia coli DSM 12847 (which is believed tc be identical ro the attached SEQ ID N0:17), the plasmid present in Escherichia coll DSM 12 84 8 (which is believed to be Identical to the attached SEQ ID N0:19), the plasmid present in Escherichia coll DSM 12849 (which is believed to be identical to the attached SEQ ID N0:21), the plasmid present in Escherichia coll DSM 12850 (which is believed to be identical to the attached SEQ ID NO:23), the plasmid present in Escherichia coli DSM 12846 (which is believed to be identical to the attached SEQ ID NO:25), the plasmid present in Escherichia coli DSM 12851 (which is believed to be identical to the attached SEQ ID NO:27), the plasmid present in Escherichia coll DSM 12852 (which is believed to be identical to the attached SEQ ID NO:29) or the plasmid present in Escherichia coli DSM 12436 (which is believed to be identical to the attached SEQ ID N0:31), e.g be a subsequence thereof, and/or by introduction of nucleotide substitutions which do not give rise to another amino acid sequence of the mannanase encoded by the DNA sequence, but which corresponds to the codons usage of the host organism intended for production of the enzyme, or by introduction of nucleotide substitutions which may give rise to a different amino acid sequence (i.e. 3 variant of the mannan degrading enzyme of the invention). POLYPEPTIDES The sequence of amino acids in positions 31-490 of SEQ ID NO: 2 is a mature mannanase sequence. The sequence of amino acids nos. 1-30 of SEQ ID NO: 2 is the signal peptide. It is believed than hue subsequence of amino acids in positions 31-330 of SEQ ID NO: 2 is the catalytic domain of the mannanase enzyme and tar the mature enzyme additionally comprises a linker in positions 331-342 and at least one C-terminal domain of unknown function in positions 343-490. Since the object of the present invention is to obtain a polypeptide which exhibits mannanase activity, the present invention relates to any mannanase enzyme comprising the sequence of amino acids nos. 31-330 of SEQ ID NO: 2r i.e. a catalytically domain, optionally operably linked, either N-terrr.inally or C-terminally, to one or rows or more than two other domains of a different functionality. The detrain having rhe subsequence of amino acids TWOS . 543-490 of SEQ ID NO: 2 is a domain of the mannanase enzyme of unknown function, this domain being highly homologous with similar domains in known mannanases, of. example 1. The sequence of amino acids in positions 32-494 of SEQ ID NO: 6 is a mature mannanase sequence. The sequence of amino acids nos. 1-31 of SEQ ID NO: 6 is the signal peptide.. It is believed that the subsequence of amino acids in positions 32-344 of SEQ ID NO:6 is the catalytic domain of the mannanase enzyme- and that the mature enzyme additionally comprises at least one C-terminal domain of unknown function in positions 345-4 94. Since the object of the present invention is to obtain a polypeptide which exhibits mannanase activity, the present invention relates to any mannanase enzyme comprising the sequence of amino acids nos. 32-344 of SEQ ID NO: 6, ice a catalytically domain, optionally operably linked, either N-terminally or C-terminally, to one or two or more than two other domains of a different functionality. The sequence of amino acids in positions 32-586 of SEQ ID NO:10 is a mature mannanase sequence. The sequence of amino acids nos. 1-31 of SEQ ID NO:10 is the signal peptide. It is believed that the subsequence of amino acids in positions 32-362 of SEQ ID NO:10 is the catalytic domain of the mannanase enzyme and that the mature enzyme additionally comprises at least one C-terminal domain of unknown function in positions 363-58 6. Since the object of the present invention is to obtain a polypeptide which exhibits mannanase activity, "he present invention relates to any mannanase enzyme comprising the sequence of amino acids nos. 32-362 of SEQ ID NO: 10, ie a catalytically domain, optionally operably linked, either N-terminally or C-terminally, to one or two or more than two other domains of a different functionality. The sequence of amino acids in positions 33-331 of SEQ ID NO:12 is a mature mannanase sequence. The sequence of amino acids nos. 1-32 of SEQ ID NO:12 is the signal peptide. It is believed that the subsequence of amino acids in positions 33-331 of SEQ ID NO:12 is the catalytic domain of the mannanase enzyme. This manuanase enzyme core comprising the sequence of amino acids nos. 33-331 of SEQ ID NO: 12, ie a catalytically domain, may or may not be operably linked, either N-terminally or C-terminally, to one or two or more than two other domains of a different functionality, ie being part of a fusion protein. The sequence of amino acids in positions 22-488 of SEQ ID NO:14 is a mature mannanase sequence. The sequence of amino acids nos. 1-21 of SEQ ID NO: 14 is the signal peptide. It is believed that the subsequence of amino acids in positions 166-488 of SEQ ID NO:14 is the catalytic domain of the mannanase and-that the mature enzyme additionally comprises at' -- '~ least one N-terminal domain of unknown function in positions 22-164. Since the object of the present invention is to obtain a polypeptide which exhibits mannanase activity, the present, invention relates to any mannanase enzyme comprising the sequence of amino acids nos. 166-488 of SEQ ID NO: 14, ie a catalytically domain, optionally operably linked, either N- terminally or C-terminally, to one or two or more lain two other domains of a different functionality. The sequence of amino acids in positions 26-369 of SEQ ID NO:16 is a mature mannanase sequence. The sequence of amino acids nos. 1-25 of SEQ ID NO:16 is the signal peptide. It is believed that the subsequence of amino acids in positions 68-369 of SEQ ID NO:16 is the catalytic domain of the mannanase enzyme and that the mature enzyme additionally comprises at least one N-terminal domain of unknown function in positions 26-57. Since rhe object of the present invention is to obtain a polypeptide which exhibits mannanase activity, the present invention relates to any mannanase enzyme comprising the sequence of amino acids nos. 68-369 of SEQ ID NO:16, ie a catalytical domain, optionally operably linked, either N-terminally or C-terminally, to one or : two or more "Chan two other domains of a different functionality. The sequence of amino acids of SEQ ID NO:18 is a partial sequence fording-part of a mature mannanase sequence. The resent invention relates to any mannanase enzyme comprising the sequence of amino acids nos. 1-305 of SEQ ID NO: IB. ; The sequence of amino acids of SEQ ID NO:20 is a partial sequence forming part of a mature mannanase sequence. The present invention relates to any mannanase enzyme comprising the sequence of amino acids nos. 1-132 of SEQ ID NO:20. The, sequence of amino acids in positions 29-320 of SEQ ID ; NO: 22 is a mature mannanase sequence. The sequence of amino acids nos. 1-28 of SEQ ID NO:22 is the signal peptide. It is believed that the subsequence of amino acids in positions- 29-320 of SEQ ID NO:22 is the catalytic domain of the mannanase enzyme. This mannanase enzyme core comprising the sequence of amino } acids nos. 29-320 of SEQ ID NO:'-22-, --ie catalytically domain, may . or may not be operably linked, either N-terminally or C-terminally, to one or two or more than two other domains of a different functionality, ie being part of a fusion protein. The sequence of amino acids of SEQ ID NO:24 is a partial - sequence forming part of a mature mannanase sequence. The present invention relates to any mannanase enzyme comprising the sequence of amino acids nos. 29-188 of SEQ ID NO:24. The sequence of amino acids in positions 30-815 of SEQ ID NO:2 6 is a mature mannanase sequence. The sequence of amino acids nos. 1-29 of SEQ ID NO:26 is the signal peptide. It is believed that the subsequence of amino acids in positions 301-625 of SEQ ID NO:26 is the catalytic domain of the mannanase enzyme and that the mature enzyme additionally comprises at least two N-terminal domain of unknown function in positions 44-166 and 195-300, respectively, and a C-terminal domain of unknown function in positions 626-815. Since the object of the present invention is to obtain a polypeptide which exhibits mannanase activity, the present invention relates to any mannanase enzyme comprising the sequence of amino acids nos. 301-625 of SEQ ID NO:26, ie a catalytical domain, optionally operably linked, either N-terminally or C-terminally, to one or two or more than two other domains of a different functionality. The sequence of amino acids in positions 35-496 of SEQ ID NO:28 is a mature mannanase sequence. The sequence of amino acids nos. 1-37 of SEQ ID NO:28 is the signal peptide- It is believed rhat tne subsequence of amino acids in positions 166- 4 96 of SEQ ID NO:28 is the catalytic domain of the mannanase enzyme and that the mature enzyme additionally comprises at least one N-terminal domain of unknown function in positions 38- 165. Since the object of the present invention is- to obtain a polypeptide which exhibits mannanase activity, the present invention relates to. any mannanase enzyme comprising the sequence of amino acids nos. 166-496 of SEQ ID NO:28, ie a catalytical domain, optionally operably linked, either N- terminally or C-terminally, to one or two or more than two other domains of -a different functionality. "' The sequence of amino acids in positions. 2 6-361 of SEQ. .ID NO:30 is a mature mannanase sequence. The sequence of amino acids nods- 1-25 of SEQ ID NO:30 is the signal peptide. It is believed that the subsequence of amino acids in positions 2 6-361 of SEQ ID NO:30 is the catalytic domain of the mannanase enzyme. This mannanase enzyme core comprising the sequence of amino acids nos. 26-361 of SEQ ID NO:30, ie a catalytical domain, mayor may not be optionally operably linked, either N-terminally ox C-terminally, to one or two or more than two other domains of a different functionality. The sequence of amino acids in positions 23-903 of SEQ ID NO:32 is a mature mannanase sequence. The sequence of amino acids nos. 1-22 of SEQ ID NO:32 is the signal peptide. It is believed that the subsequence of amino acids in positions 593-903 of SEQ ID NO: 32 is the catalytic domain of the iTiannanase enzvTTie and that the mature enzyme additionally comprises at least three N-terminal domains of unknown function in positions 23-214, 224-424 and 434-592, respectively. Since the object of rhe present invention is to obtain a polypeptide which exhibits mannanase activity, the present invention relates to any mannanase enzyme comprising the sequence of amino acids nos. 593-903 of SEQ ID NO:32, ie a catalytical domain, optionally operably linked, either N-terminally or C-terminally, to one or z-'^-c cr more than two ether domains of a different functionality. The present invention also provides mannanase polypeptides are substantially hoinologous to the polypeptides of SEQ ID N0:2, SEQ ID N0:.6, SEQ ID NO:10, SEQ ID N0:12, SEQ ID N0:14, SEQ ID N0:16, SEQ ID N0:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30 and SEQ ID NO:32, respectively, and species homologs (paralogs or orthodox) thereof. The term "substantially homologous" is used herein to denote polypeptides having 65%, preferably at least 70%, more preferably at least 75%, more preferably at least 80%, more preferably at least 85%, and even more preferably at least 90%, sequence identity to the sequence shown in amino acids nos. ) 33-340 or nos. 33-490 of SEQ ID N0:2 ox their orthologs or paralogs; or to the sequence shown .ITI amino acids nos. 32-344 or nos. 32-494 of SEQ ID NO:6 or their orthologs or paralogs; or to the sequence shown in amino acids nos. 32-362 or nos. 32-58 6 of SEQ ID NO:10 or their orthologs" or paralogs; or to the sequence : shown in amino acids nos. 33-331 of SEQ ID N0:12 or its orthologs or paralogs; cry to the sequence shown in amino acids nos. 166-488 or nos. 22-488 of SEQ ID NO:14 or their orthologs or paralogs; or to the sequence shown in amino acids nos. 68-369 or nos. 32-369 of SEQ ID NO:16 or their orthologs or paralogs; or to the sequence shown in amino acids nos. 1-305 of SEQ ID NO: 18 or its orthologs or paralogs; or to the sequence shown in amino acids nos-. 1-132 of SEQ ID NO: 20 or its orthologs or paralogs; or to the sequence shown in amino acids nos. 29-320 of SEQ ID NO:22 or its orthologs or paralogs; or to the sequence shown in amino acids nos. 29-188 of SEQ ID NO:24 or its orthologs or paralogs; or to the sequence shown in amino acids nos. 301-625 or nos. 30-625 of SEQ ID NO:26 or their orthologs or paralogs; or to the sequence shown in amino acids nos., 166-.496 or nos. 38-496 of SEQ ID NO:28 or their orthologs or paralogs; or to the sequence shown in amino acids nos. 2 6-361 of SEQ ID NO:30 or its orthologs or paralogs; or to rhe sequence shown in amino acids nos. 593-903 or nos. 23-903 of SEQ ID NO:32 or their orthologs or paralogs. Such polypeptides will more preferably be at least 95% identical, and most preferably 98% or more identical to the sequence shown in airier acids nos. 31-330 or nos - 31-4-90 of SEQ ID N0:2 or its orthologs or paralogs; or to the sequence shown in amino acids nos. 32-344 or nos. 32-494 of SEQ ID NO: 6 or its orthologs or paralogs; or to the sequence shown in amino acids nos. 32-362 or. nos. 32-586 of SEQ ID NO: 10 or- its orthologs or paralogs; or to the sequence shown in amino acids nos. 33-331 of SEQ ID NO:12 or its orthologs or paralogs; or to the sequence shown in amino acids nos. 166-488 or nos. 22-488 of SEQ ID NO:14 or its orthologs or paralogs; or to the sequence shown in amino acids nos. 68-369 or nos. 32-369 of SEQ ID N0:16 or its orthologs OT' the sequence shown in amino acids nos. 1-305 o± SEQ ID NO:18 or its orthologs or paralogs; or to the sequence shown in amino acids nos. 1-132 of SEQ ID NO:20 or its orthologs or paralogs; or to the sequence shown in amino acids nos... 29-320 of SEQ ID NO:22 or its orthologs or paralogs; or to the sequence shown in amino acids nos. 29-188 of SEQ ID NO;2 4 or its orthologs or paralogs; or to the sequence shown in amino acids nos. 301-625 or nos. 30-625 of SEQ ID NO:26 or its orthologs or paralogs; or to the sequence shown in amino acids nos. 166-496 or nos. 38-496 of SEQ ID NO:28 or its orthologs or paralogs; or to the sequence show’s in amino acids nos. 26-361 of SEQ ID NO:30 or its orthologs or paralogs; or to the sequence shown in amino acids nos. 593-903 or nos. 23-903 of SEQ ID NO:32 or its orthologs or paralogs. Percent sequence identity is determined by conventional methods^ by means of computer programs known in the art such as GAP provided in the GCG program package (Program Manual for the Wisconsin Package/ Version 8, August 1-994, Genetics Computer Group 575 Science Drive Madison, Wisconsin, USA 53711) as disclosed in Needle man, S.B. and Wunsch, CD., (1970), Journal of Molecular Biology, 48, 443-453, which is hereby incorporated by reference in its entirety. GAP is used with the following settings for polypeptide sequence comparison: GAP creation penalty of 3.0 and GAP extension penalty of 0.1. Sequence identity of polynucleotide molecules is deterrence by similar methods using GAP with the following settings for DNA sequence comparison: GAP creation penalty of 5.0 and GAP extension penalty of 0.3. The enzyme preparation of the invention is preferably derived from a microorganism, preferably from a bacterium, an archea or a. fungus,, especially from a bacterium such as a bacterium belonging to Bacillus preferably to a Bacillus strain which :may be selected from the group consisting of the species Bacillus sp. and highly related Bacillus species in which all species preferably are at least 95%, even more preferably at least 98%, homologous to Bacillus sp. 1533, Bacillus n'alodurans or Bacillus sp. AAI12 based on aligned 'I6S'rDj^A sequences. These species are claimed based on phylogenic relationships identified from aligned 16S cDNA sequences from RDP (Ribosomal Database Project) {Bonne L. Media, Nails Larson, Michael J. McCaughey, Ross Overbid, Gary J. Olsen, Karl Feel, James Blindly, and Carl R. Woese, Nucleic Acids Research, 1994, Vol. 22, Nol7, p. 3485-3487, The Ribosomal Database Project). The alignment was based on secondary structure. Calculation of sequence simularities were established using the ""^Full matrix calculation" with default settings of the neighbor joining method integrated in the ARE program package (Oliver Stunk and Wolfgang Ludwig, Technical University of Munich, Germany). Information derived from table II are the basis for the claim for all family 5 mannanases from the highly related Bacillus species in which all species over 93% homologous to Bacillus sp. 1533 are claimed. These include: Bacillus sporo-thermoduransr Bacillus acidophilus Bacillus pseudoalcalophilus and Bacillus classic- See Figure 1: Phylogenic tree generated from ARP program relating closest species to Bacillus sp. 1633. The 16S RNA is shown in SEQ ID NO:33. Table II: 16S ribosomal RNA homology index for select Bacillus species Other useful family 5 mannanases are those derived from the highly related Bacillus species in which all species show more than 93% homology to Bacillus halodurans based on aligned 16S sequences. These Bacillus species include: Sporolactobacil- lust leaves Bacillus agaradhaerens and Marinococcus homophiles. See Figure 2: Phylogenic tree generated from ARP program relating closest species to Bacillus halodurans- Table III: 16S ribosomal RNA homology index for selected Bacillus species SplLaev5 BaiSpec6 Bissell MaoHalo2 NN SplLaev3 90.98% 87.96% 85.94% 91.32% NK - donor organism of the invention (B. halodurans) Other useful family 5 mannanases are those derived from a strain selected from the group consisting of the species Bacillus agaradhaerens and highly related Bacillus species in which all species preferably are at least 95%, even more preferably at least 98%, homologous to Bacillus agaradhaerens^ DSM 8721;. based on aligned 16S cDNA sequences. Useful family 2 6 mannanases are for example those derived from the highly related Bacillus species in which all species over 93% nomclcgous to Bacillus sp. AA112 are claimed. These inc- use : Bacillus sporothermodurans, Bacillus acidophilus Bacillus pseudoalcalophilus and Bacillus clause- See Figure 3: Phylogenic tree generated from ARP program relating closest species to Bacillus sp, Ail 12. The 16S RNA is shown in SEQ ID NO:34. Table IV: 16S ribosomal RNA homology index for selected Bacillus species other useful family 26 mannanases are those derived from a strain selected from the group consisting of the species Bacillus licheniformls and highly related Bacillus species in which all species preferably are at least 95%, even more preferably at least 98%, homologous to Bacillus licheniformls based on aligned 16S rDNA sequences. Substantially homologous proteins and polypeptides are char-cauterized as having one or more amino acid substitutions, deletions or additions. These changes are preferably of a minor nature, that is conservative amino acid substitutions (see Table 2; and other substitutions that do not significantly affect the folding or activity of the protein or polypeptide; small deletions, -cynically of one to about 30 amino acids; and small amino- or carboxyl-terminal extensions, such as an amino-terminal motioning residue, a small linker peptide of up to about 20-25 residues, or a small extension that facilitates purification -an affinity tag), such as a ply-histidine tract, protein A (Nilsson et al . , EMBO J. 4_:1075, 1985; Nilsson et al . , Methods Enzvmol. 198:3, 1991. See, in general Ford et al.. Protein Expression and Purification 2_: 95-10-7, 1991, which is incorporated herein by reference. DNAs encoding affinity tags are available from commercial suppliers (e.g., Pharmacia Biotech, Piscataway, NJ; New England Bola’s, Beverly, MA). However, even though the changes described above preferably are of a minor nature, such changes may also be of a larger nature such as fusion of larger polypeptides of up to 300 amino acids or more both as amino- or carboxyl-terminal extensions to a Mannanase polypeptide of the invention. Table 1 Conservative amino acid substitutions Basic: arginine lysine Histidine Acidic: glutamic acid asp artic acid Polar: glutamine asparagine Hydrophobic: leonine isoleucine valise Aromatic: phenylalanine tryptophan tyrosine Small: glycine alanine serine threonine merhionine In addition to the 2 0 standard amino acids, non-standard amino acids (such as 4-hydroxyproline, 6-N-methyl lysine, 2-aminoisobutyric acid, isohaline and a-methyl serine) may be substituted for amine acid residues of a polypeptide according ~o the invention. A lairised of non~conservative amino acids, amino acids that are not encoded by the genetic code, and unnatural amino acids may be substituted for amino acid residues . '^Unnatural amino acids' have been modified after protein synthesis, and/or have a chemical structure in their side chain (s). different from that of the standard amino acids. Unnatural amino acids can be chemically synthesized, or preferably, are commercially available, and include pipe colic acid, thiazolidine carboxylic acid, dehydroproline, 3- and 4-methylproline, and 3,3-dimethylproline. Essential amino acids in the mannanase polypeptides of the present invention can be identified according to procedures known in the art, such as site-directed autogenesis or ai'anine-' scanning autogeneses (Cunningham and Wells, Science 24 4:. 1081-1085, 1989) . In the latter technique, single alanine mutations are introduced at every residue in the molecule, and the resul-r,ant mutant molecules are tested for biological activity (i. e mannanase activity) to identify amino acid residues that are critical to the activity of the molecule. See also, Hilton et al., J, Biol. Chem. 271:4699-4708, 1996. The active site of the enzyme or other biological interaction can also be determined by physical analysis of structure, as determined by such techniques as nuclear magnetic resonance, crystallography, electron diffraction or photo affinity labeling, in conjunction with mutation of putative contact site amino acids. See, for example, de Voss et al., Science 255:306-312, 1992; Smith et al., J, Mol. Biol. 211:899-904, 1992; Woodier et al., FEES Lett. 309:59-64, 1992. The identities of essential amino acids can also be inferred from analysis of homologies with polypeptides which are related to a polypeptide according to the invention. Multiple amino acid substitutions can be made and tested using known methods of autogeneses, recombination and/or shuffling followed by a relevant screening procedure, such as those disclosed by Reidhaar-Olson and Sauer (Science 241:53-57, 1988), Bowie and Sauer (Proc. Natl. Acad. Sci. USA 86:2152-2156, 1989), W095/17413, or WO 95/22625. Briefly, these authors disclose methods for siiriultaneously randomizing two or more pcsix:ions in 5 polypeptide, or recombination/shuffling of different mutations fW095/174i3, W095/22625), followed by selecting for functional a polypeptide, and then sequencing the mutagenized polypeptides to determine the spectrum of allowable substitutions at each position. Other methods that can be used include phage display {e.g., Lowman et al., Biochem. 1£:10832-10837, 1991; Lander et al., U.S. Patent No. 5,223,409; Huse, WIPO Publication WO 92/06204) and region-directed autogeneses (Derbyshire et al., Gene £6:145, 1986; Ner et al., DNA 2:127, 1988) . Autogeneses/shuffling methods as disclosed above can be combined with high-throughput, automated screening methods to detect activity of cloned, mutagenized polypeptides in host cells. Mutagenized DNA molecules.that encode active polypeptides can be recovered from the host cells and rapidly sequenced using modern equipment. These methods allow the rapid determination of ~he importance of individual airing acid residues in a polypeptide of interest, and can be applied to polypeptides of unknown structure. Using the methods discussed above, one of ordinary skill in rhe art can identify and/or prepare a variety of polypeptides that are substantially homologous to residues 33-340 or 33-490 of SEQ ID N0:2; or to residues 32-344 or 32-494 of SEQ ID N0:6; or to residues 32-362 or32-586 of SEQ ID NO:10; or to residues 35-331 of SEQ ID N0:12; or to residues 166-488 or 22-488 of SEQ ID N0:14; or to residues 68-369 or 32-369 of SEQ ID N0:16; or to residues 1-305 of SEQ ID N0:18; or to residues 1-132 of SEQ ID NO:20; or to residues 29-320 of SEQ ID NO:22; or to residues 29-136 of SEQ ID NC:24; or to residues 301-625 or 30-625 of SEQ ID NG:26; or ro residues 166-496 or 38-496 of SEQ ID NO:28; or to residues 26-361 of SEQ ID NO:30; or to residues 593-903 or 23-9C3 of SEQ ID NO:32 and retain the mannanase activity of the wild-type protein. The mannanase enzyme of the invention may, in addition to the enzyme core comprising the catalytically domain, also comprise a cellulose binding domain (CBD), the cellulose nine in g domain and Enzvmol core (the catalytically active domain) of the enzyme being operably linked. The cellulose binding domain (CED) may exist as an integral par of ::he encoded enzyme, or a CBD from another origin may be introduced into the mannan degrading, enzyme thus creating an enzyme hybrid. In this context, the term "'cellulose-binding domain" is intended to be understood as defined by et al. 'Cellulose-Binding Domains: Classification and Properties" in "Enzymatic Degradation of Insoluble Carbohydrates", John N. Saddler and Michael H. Fenner (Eds.), ACS Symposium Series, No. 618, 1996. This definition classifies more than 120 cellulose-binding domains into 10 families (I-X), and demonstrates that C3Ds are found” in various enzymes such as cellulases, xylanase, mannanases, arabinofuranosidases, acetyl esterase’s and chattiness. CBDs have also been found in algae, e.g. the red alga Porphyra purposes as a non-hydrolytic polysaccharide-binding protein, -see Time et al. , O]D. cit. However, most of the CBDs are from cellulases and xylanase, CBDs are found at the N and C termini of proteins or are internal. Enzyme hybrids are known in the art, see e.g. WO 90/00609 and WO 95/16782, and may be prepared by transforming into a host cell a DNA construct comprising at least a fragment of DNA encoding the cellulose-binding domain liased, with or without a linker, to a DNA sequence encoding the mannan degrading enzyme and growing the host cell to express the fused gene. Enzyme hybrids may be described by the following formula: CBD - MR - X wherein. CBD is the N-terminal or the C-terminal region of an amino acid sequence corresponding to at least the cellulose-binding domain; MR is the middle region (the linker), and may be a bond, or a short linking group preferably of from about 2 to about 100 carbon atoms, more preferably of from 2 to 40 carbon atoms; or is preferably from about 2 to about 100 amino acids, more preferably of from 2 to 40 amino acids; and X is an N-terminal or C-terminal region of the mannanase of the invention. SEQ ID NO:4 discloses the amino acid sequence of an enzx-nme hybrid of a mannanase benzene core and a CBD. Preferably, the mannanase enzyme of the present invention has its maxim am cat a lyric activity at a kPa of at least 7, mere preferably of at least 8, more preferably of at least 8.5, more preferably of at least 9, more preferably of at least 9.5, more preferably of at least 10, even more preferably of at least 10-5, especially of at least 11; and preferably the maximum activity of the enzyme is obtained at a temperature of at least 40°C, more preferably of at least 50°C, even more preferably of at least 55°C. Preferably, the cleaning composition of the present invention provides, eg when used for treating fabric during a washing cycle of a machine washing process, a washing solution having a pH typically between about 8 and about 10.5. Typically, such a Washing solution is used at temperatures between about 20' and about 95°C, preferably between about 20' and about 60°C, preferably between about 2 0°C and about DOE’S. PROTEIN PRODUCTION: The proteins aid polypeptides, of the present invention, including full-length proteins, fragments thereof and fusion proteins, can be produced in genetically engineered host cells according to conventional techniques. Suitable host cells are those cell types that can be transformed or transfected with exogenous DNA and grown in culture, and include bacteria, fungal cells, and cultured higher eukaryotic cells. Bacterial cells, particularly cultured cells of gram-positive organisms, are preferred. Gram-positive cells from the genus of Bacillus are especially preferred, such as from group consisting of Bacillus subtonics. Bacillus lentos . Suitable procedures for transformation of Aspergillums host cells are described in EP 238 023 and Elton et ai., 1984, Proceedings of the National Academy of Sciences USA 81:1470-1474, A suitable method of transforming Fusariijm species is described by Malaria et la.l 1989, Gene 78:147-156 or in cop ending US Serial No. 08/269,449. Yeast may be transformed using the procedures described by Becker and Guarantee, in Abelson’s, J.N. and Sermon, M.I., editors. Guide to Yeast Genetics and Molecular Biology, Methods in Enzymology, Volume 194, pp 182-187, Academia Press, Inc., New York; Ito et al., 1983, Journal of Bacteriology 153:163; and Hinnen et a., 1978, Proceedings of the National Academy of Sciences USA 75:1920. Mammalian cells may be transformed by direct uptake using the calcium phosphate precipitation method of Graham and Van dour Eb [1378, Virology 52:546). Techniques for manipulating cloned DNA molecules and introducing exogenous DNA into a variety of host cells are disclosed by Sambrook et al.. Molecular Cloning: A Laboratory Manual, 2nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 1989; Ausubel et al. (eds.), Current Protocols in Molecular Biology, John Wiley and Sons, Inc., NY, 1987; and '^Bacillus s-utilise and Other Gram-Positive Bacteria", Sonneteer et al., 1993, American Society for Microbiology, Washington D.C., which are incorporated herein by reference. In general, a DNA sequence encoding a mannanase of the present invention is operably linked to other genetic elements required for ins expression, generally including a transcription promoter and terminator within an expression vector. The vector will also commonly contain one or more selectable markers and one or more origins of replication, although those skilled in she art will recognize that within certain systems selectable markers gray be provided on separate vectors, and replication of the exogenous DNA may be provided by integration into the host cell venom. Selection of urometers, terminators, selectable markers, vectors and other elements is a matter of routine design within the level of ordinary skill in the art. Many such elements are described in the literature and are available through commercial suppliers. To direct a polypeptide into the secretory pathway of a host cell, a secretory signal sequence (also known as a leader sequence, prepare sequence or pre sequence) is provided in the expression vector. The secretory signal sequence may be that of the polypeptide, or may be derived from another secreted protein or synthesized de novo- Numerous suitable secretory signal sequences are known m the art and reference is made to '"Bacillus subtitles and Other Gram-Positive Bacteria", Sonneteer et al., 1993, American Society for Microbiology, Washington D.C.; and Cutting, S. M.(eds.) "Molecular Biological Methods for. Bacillus", John Wiley and Sons, 1990, for further description of suitable secretory signal sequences especially for secretion in a Bacillus host cell. The secretory signal sequence is joined to the DNA sequence in the correct reading frame. Secretory signal sequences are commonly positioned 5 * to the DNA sequence encoding the polypeptide of interest, although certain signal se-quinces may be positioned elsewhere in the DNA sequence of interest (see, e.g., Welch et al., U.S. Patent No. 5,037,743; Holland et al., U.S. Patent No. 5,143,830). ,The expression vector of the invention may be any expression vector that is conveniently subjected to recombinant DNA procedures, and hue choice of vector will often depend on rhe host cell into which the vector it is to be introduced. Thus, the verse may be an autonomously replicating vector, i.e. a vector which exists as an extrachromosomal entity, the replication of which is independent of chromosomal replication, e.g. a plasmid. Alternatively, the vector may be one which, when introduced into a host cell, is integrated into the host cell genome and replicated together with the chromosome(s) into which it has been integrated. Examples of suitable promoters for use -in filamentous fungus host cells are, e.g. the ADH3 promoter. [McKnight et al., The EM30-J. ^ (1985), 2093 - 2099) or the Transformed or transfected host cells are cultured according our conventional procedures in a culture medium containing nutrients and other components required for the growth of the chosen host cells. A variety of suitable media, including defined media and complex media, are known in the art and generally include a carbon source, a nitrogen source, essential amino acids, vitamins and minerals. Media may also contain such components as growth factors or serum, as required. The growth medium will generally select for cells containing the exogenously added DNA by, for example, drug selection or deficiency in an essential nutrient which is complemented by the selectable inerter carried on the expression vector or co-transfected into the host cell. PROTEIN ISOLATION When the expressed recombinant polypeptide is secreted the polypeptide may be purified from the growth media. Preferably ~he expression host cells are removed from the media before purification of the polypeptide (e.g. by centrifugation). When the expressed recombinant polypeptide is not secreted from the host cell, the host cell are preferably disrupted and rhe polypeptide released into an aqueous "extract" which is the first stage of such purification techniques. Preferably the expression host cells are collected from the media before the cell disruption (e.g. by centrifugation). The cell disruption may be performed by conventional techniques such as 'by lysczyme digestion or by forcing the cells "hrough high pressure. See (Robert K. Scobes, Protein Purification, .Second edition, Springer-Verlag) for further description of such cell disruption techniques. Whether or not the expressed recombinant polypeptides (or chimeric polypeptides) is secreted or not it can be purified using fractionation and/or conventional purification methods and media. Ammonium sulfate precipitation and acid or chaotrope extraction may be used for fractionation of samples. Exemplary purification steps may include hydroxyapatite, size exclusion, FPLC and reverse-phase high performance liquid chromatography. Suitable anion exchange media include derivalized dextrin’s, agarose, cellulose, polyacryamido, specialty" silica, and the like. PEI, DEA-E, QAE and Q derivatives are preferred, with DEAE Fast-Flow Sparse (Pharmacia, Piscataway, NJ) being particularly preferred. Exemplary chromatographic media include those media■ derivatized with phenyl, butyl, or octyl groups, such as Phenyl-Spheres FF (Pharmacia), Toy pearl butyl 650 (Togo Hams, Montgomery vi lie, PA), Ocryl-Sepharose (Pharmacia) and the like; or polyacrylic resins, such as Amberchroxn CG 71 (Torso Haws) and the like. Suitable solid supports include glass beads^ silica-based resins, cellulosic resins, agarose beads, cross-linked agarose beads, polystyrene beads, cross-linked polyacrylamide resins and rhe like that are insoluble under the conditions in which they are to be used. These supports may be modified with reactive ' groups that allow attachment of proteins by amino groups, car-boxyl groups, sulfhydryl groups, hydroxyl groups and/or carbohydrate moieties. Examples of coupling chemistries include cyanogen bromide activation, N-hydroxysuccinimide activation, epoxide activation, sulfhydryl activation, hydrazide activation, and carboxyl and amino derivatives for carbodiimide coupling chemis-rries. These and other solid media are well known and widely used in the art, and are available from commercial suppliers. Selection of a particular method is a matter of routine design and is determined in part by the properties of the chosen support. See, for example, Affinitv Chromatography: Principles & Mei-hods, PharTTLccia LKE Biotechnology, Upsilon, Sweden, 198 6. Polypeptides of the invention or fragments thereof may also be prepared through chemical synthesis. Polypeptides of the invention may be monomers or muleteers; glycosylated or non-glycosylated; paginated or non-paginated; and may or may not include an initial merhionine amino acid residue. Based on the sequence information disclosed herein a full length DNA sequence encoding a mannanase of the invention and comprising the DNA sequence shown in SEQ ID No 1, at least the DNA sequence from position 94 to position 990, or, alternatively, the DNA sequence from position 94 to position 1470, may be cloned. ‘Likewise may be cloned a full length DNA sequence ■ -encoding a mannanase of the invention and comprising the DNA sequence shown in SEQ ID No 5, at least the DNA sequence from position 94 to position 1032, or, alternatively, the DNA sequence from position 94 to position 14 82; and a full length DNA sequence encoding a mannanase of the invention and comprising the DNA. sequence shown in SEQ ID No 9, at least the DNA. se- quince from position 94 to position 1086, or, alternatively, hued DNA sequence from position 94 to position 1761; and a full length DNA sequence encoding a iTLannanase of the invention and comprising the DNA sequence shown in SEQ ID No 11, at least the DNA sequence from, position 97 to position 993; and a full length DNA sequence encoding a mannanase of the invention and comprising the DNA sequence shown in SEQ ID No 13, at least the DNA sequence from position 4 98 to position 14 64, or, alternatively, the DNA sequence from position 64 to position 1464; and a full length DNA sequence encoding a mannanase of the invention and comprising the DNA sequence shown in SEQ ID No 15, at least the DNA sequence from position 204 to position 1107, or, alternatively, the DNA sequence from position 76 to position 12;"'; and a DNA sequence partially encoding a mannanase of the invention and comprising the DNA sequence shown in SEQ ID No I" and a DNA sequence partially encoding a mannanase of the :invention and comer’s inc the DNA sequence shown in SEQ ID No ; and a full length DNA sequence encoding a mannanase of the invention and comprising the DNA sequence shown in SEQ ID No 21.. at least the DNA sequence from position 8 to position 960; and a DNA sequence partially encoding a mannanase of the invention and comprising the DNA sequence shown in SEQ ID No 23; and a full length DNA. sequence encoding a mannanase of the invention and comprising the DNA sequence shown in SEQ ID No 25, at least the DNA sequence from position 904 to position 1875, or, alternatively, the DNA sequence from position 88 to position 2 44 5; and a full length DNA sequence encoding a mannanase of the invention and comprising the DNA sequence shown in SEQ ID No 27, at least the DNA sequence from position 498 to position 1488, or, alternatively, the DNA sequence -from position 112 to posi-cion 1488; and a full length DN^' sequence encoding a mannanase of the invention and comprising the DNA sequence shown in SEQ ID No 29, at least the DNA sequence from position 79 to pSe It ion 1083; and a full length DNA sequence encoding a iTLannanase of the invention and comprising the DNA sequence shown in SEQ ID No 31, at least the DNA sequence from position 17 7 9 to position 2709, or, alternatively, the DNA sequence from position 67 to position 2709. Cloning is performed by standard procedures known in the are such as by, ? preparing a genomic library from a Bacillus strain, especially a strain selected from 3. sp. 1633, B. sp. AAI12, B. sp. AA349. Bacillus agaradhaerensr Bacillus halodurans Bacillus clause and Bacillus licheniformis, or from a fungal s-rain, especially the strain Hum cola insulin’s ? paring such a library on suitable substrate plates; ? a clone comprising a polynucleotide sequence of he invention by standard hybridization techniques using a probe based on any of the sequences SEQ IDMOs. 1, 5, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29 or 31; or by ? identifying a clone from said genomic library by an Inverse ?CR strategy using primers based on sequence information from SEQ ID No 1, 5, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29 or 31. Reference is made to M.J. McPherson et al. ('PCR A practical approach" Information Press Ltd, Oxford England) for further details relating to Inverse PCR. Based on the sequence information disclosed herein (SEQ ID Nos 1, 2, 5, 6, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 2C, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32) is it routine work for a person skilled in the art to isolate homologous polynucleotide sequences encoding homologous mannanase of "he invention by a similar strategy using genomic libraries from related microbial organisms, in particular from genomic libraries from other strains of the genus Bacillus such as alkalophilic species of Bacillus sp-r or from fungal strains such as species of Hum cola. Alternatively, the DNA encoding the mannan or galactoman-nan-degrading enzyme of the invention may, in accordance with well-known procedures, conveniently be cloned format a suitable source, such as any of the above mentioned organisms, by use of synthetic oligonucleotides probes prepared on the basis of the DNA. sequence obtainable from the plasmid present any of 'the strains Escherichia coli DSM 12197, DSM 12180, DSM 12433, DSM 12441, DSM 9984, DSM 12432, DSM 12436, DSM 12846, DSM 12847, DSM 12848, DSM 12849, DSM 12850, DSM 12851 and DSM 12852. Accordingly, ~he polynucleotide molecule of the invention nay be isolated from any of Escherichia coli, DSM 12197, DSM 12180, DSM 12433, DSM 12441, DSM 9984, DSM 12432, DSM 12436, DSM 12846, DSM 12847, DSM 12848, DSM 12849, DSM 12850, DSM 12c51 and DSM 12852, in which the plasmid obtained by cloning such as described above is deposited. Also, the present invention relates to an isolated substantially outré biological culture of any of the strains Escherichia coli, DSM 12197, DSM 12150, DSM 12433, DSM 12441, DSM 9984, DSM 12432, DSM 12436, Day. 12546, DSM 12847, DSM 12848, DSM 12849, DSM 12850, DSM 12S51 and DSM 12852. In the present context, the term 'enzyme preparation" is intended to mean either a conventional enzymatic fermentation product, possibly isolated and purified, from a single species of a microorganism, such preparetlDn usually comprising a enzwaatic activities; or a mixture of monocomponent enzw;es, preferably enzymes derived from, bacterial or fungal species by using conventional recombinant techniques, which enzymes have been fermented and possibly isolated and purified separately and which may originate from different species, preferably fungal or bacterial species; or the fermentation product of a microorganism which acts as a host cell for expression of a recombinant mannanase, but which microorganism simultaneously produces other enzymes, e.g. pectin degrading, enzymes, proteases, or cellulases, being naturally occurring fermentation products of the microorganism, i.e. the enzyme complex conventionally produced by the corresponding naturally occurring microorganism. The mannanase preparation of the invention may further comprise one or more enzymes selected from, the group consisting of proteases, cellulases (endo-p-l,4-Glucanases), p-glucanases ;,endo-p-1, 3(4) -glucanases) , lipases, cutinases, peroxidases, jackasses, amylases, glucoamylases, pettiness, reductase, In another aspect, the present invention also relates to a method of producing the enzyme preparation of the invention, the ziernod comprising culturing a microorganism, eg a wild-type strain, capable of producing the mannanase under conditions permitting she production of the enzyme, and recovering the enzyme from the culture. Culturing may be carried out using conventional fermentation techniques, e.g. culturing in shake flasks cry terminators with agitation to ensure sufficient aeration on a growth medium, inducing production of the manganese densities. The growth medium may contain a conventional N-source such as peptone, yeast extract or calamine acids, a reduced antigun of a conventional C-source such as dextrose or sucrose, and an inducers such as guar gum or locust bean gum. The recovery may be carried out using' conventional techniques, e.g. separation of bio-mass and supernatant by centrifugation or filtration, recovery of the supernatant or disruption of cells if the enzyme of interest is intracellular, perhaps followed by further purification as described in EP 0 4 06 314 or by crystallization as described in WO 97/15660. Examples of useful bacteria producing the enzyme or the enzyme preparation of the invention are Gram positive bacteria, preferably from the Bacillus/Lactobacillus subdivision, preferably a strain from, the genus Bacillus more preferably a strain of Bacillus spin yet another aspect, the present invention relates to an isolated mannanase having the properties described above and which is free from homologous impurities, and is pr6du'fced using conventional recombinant techniques. IMMUNOLOGICAL CROSS-REACTIVITY Polyclonal antibodies to be used in determining immunological crcss-reactivixy may be prepared by use of a purified mannanase enzyme. More specifically, antiserum against he n-iTLannanase cN the invention may be raised by immunizing rabbirs 'or other rodents) according to the procedure described by N. Axels et al. in: A Manual of Quantitative Iinmunoelectrophoresis, Blackwell Scientific Publications, 1973, Chapter 23, or A. Johnstone and R. Thorpe, Immunechemistry in Practice, Blackwell Scientific Publications, 1982 (more specifically p. 27-31). Purified Immunoglobulin may be obtained from the antisera, for example by salt precipitation ((NHs SO,), followed by dialysis and ion exchange chromatography, e.g. on DEAE-Spandex. Immunochemical characterization of proteins may be done either by Outcherlony double-diffusion analysis (O. Cuchxeriony in: Handbook of Experimental Immunology (D .M. veer, Zed.), Blackwell Scientific Publications, 1967, pp. 655-706), by crossed Immunoelectrophoresis {N. Axels et al., supra. Chapters 3 and 4), or by rocket Immunoelectrophoresis (N. Axles et al., Chapter 2). Use ±n the detergent industry In further aspects, the present invention relates to a detergent composition comprising the mannanase or mannanase preparation of the invention, to a process for machine treatment of fabrics "comprising treating fabric during a wasting "cycle of 'a machine washing process vita a washing solution containing the manganese or mannanase preparation of the invention, and to cleaning compositions, including laundry, dishwashing, hard surface cleaner, personal cleansing and oral/denial compose-"ions, comprising a mannanase and optionally another enzvTTie selected among cellulases, amylases, pectin degrading enzymes and xyloglucanases and providing superior cleaning performance, i.e. superior stain removal, dingy cleaning and whiteness maintenance. Without being bound to this theory, it is believed that the iTiannanase of the present invention is capable of effectively degrading or hydrolyzing any soiling or spots containing galactomannans and, accordingly, of cleaning laundry comprising such sailings or sots. The clearing compositions of the invention must contain at leans one additional detergent component. The precise nature of hose additional components, and levels of incorporation thereof will depend on the physical form of the composition, and the nature cN the cleaning operation for which it is to be used. The cleaning compositions of the present invention preferably further comprise a detergent ingredient selected from a selected surfactant, another enzyme, a builder and/or a bleach s V s t me. The cleaning compos it ions according to the invention can be liquid, paste, gels., bars, tablets, spray, foam, powder or granular. Granular compositions can also be in '^compact" form and the liquid compositions can also be in a "concentrated" form. The compositions of the invention may for example, be -formulated as hand and machine dishwashing compositions, hand and machine laundry detergent compositions including laundry additive compositions and compositions suitable for use. in the soaking and/or pretreatment of stained fabrics, rinse added fabric softener compositions, and compositions for use in general household hard surface cleaning operations. Compositions containing such carbohydr-as-es- can also -be formulated as sanitization products, contact lens cleansers and health and beauty care products such as oral/dental care and personal cleaning compositions. when formulated as compositions for use in manual dishwashing methods the compositions of the invention preferably contain a surfactant and preferably other detergent compounds selected from organic polymeric compounds, suds enhancing agents, group II metal ions, solvents, hydrotrope and additional enzymes. When formulated as compositions suitable for use in a laundry machine washing method, the compositions of the invent-lion preferably contain both a surfactant and a builder compound and additionally one or more detergent components preferably selected from organic polymeric compounds, bleaching agents, additional enzymes, suds suppressors, dispersants, lime-soap dispersant5, soil suspension and anti-redeposirion agents and corrosion inhibitors. Laundry compositions can also contain 5cfrening agents, as additional detergent components. Such curiosities containing carbohydrate can provide fabric cleaning, stain removal, whiteness maintenance, softening, colour appearance, dye transfer inhibition and sanitization when formulated as laundry detergent compositions. The compositions of the invention can also be used as detergent additive products in solid or liquid form. Such additive products are intended to supplement or boost the performance of conventional detergent compositions and can be added at any stage of the cleaning process. If needed the density of the laundry detergent compositions herein ranges from 400 to 1200 g/litre, preferably 500 to 950 g/liter of composition measured at 20*^0- The "compact" form of the compositions herein is best reflected by density and, in terries of composition, by the amount of inorganic filler salt; inorganic filler salts are conventional ingredients of detergent compositions in powder form; in conventional detergent compositions, the filler salts are present: in substantial amounts typically 17-35% by weight of the ictcil-'CCTuposition. In the compact impositions, the filler -as-it is present in amounts not exceeding 15% of the total composi-ricn, preferably not exceeding 10%, most preferably not exceeding 5% by weight of the composition. The inorganic filler salts, such as meant in the present compositions are selected from the alkali and alkaline-earth-metal salts of sulphate and chlorines . A preferred filler salt is sodium sulphate. Liquid detergent compositions according to the present invention can also be in a "concentrated furry"; in such case the liquid detergent compositions according the present invention will contain a lower amount of water, compared to conven-lional liquid detergents. Typically the water content of the concentrated liquid detergent is preferably less than 40%, more preferably less than 30%, most preferably less than 20% by weight of rhe detergent composition. Cleaning compositions Surfactant system The. cleaning or detergent compositions according to the present invention comprise a surfactant system., wherein the surfactant can be selected from nonionic and/or anionic and/or cationic and/or impolitic and/or zwitterionic and/or semi-polar surfactants. The surfactant is typically present at a level from. 0.1% re 60% by vjeight. The surfactant is preferably formulated to be compatible with enzyme hybrid and enzyme components present in the composition. In liquid or gel compositions the surfactant is most preferably formulated in such a way that it promotes, or at least does not degrade, the stability of any enzyme hybrid or enzyme in these compositions. Suitable systems for use according to the present invention comprise as a surfactant one or more of the nonionic and/or anionic surfactants described herein. Polyethylene, polypropylene, and polybutylene oxide condemn-sates of alkyl phenols are suitable for use as the nonionic surfactant of the surfactant systems of the present invention, with the polyethylene o-x-ids'condensates being preferred. These compounds include the condensation products of alkyl phenols having an alkyl group containing from about 6 to about 14 carbon atoms, preferably from about 8 to about 14 carbora. atoms, in either a straight chain or branched-chain configuration with the alkylene oxide. In a preferred embodiment, the ethylene oxide is resents in an amount equals to from, about 2 to about 25 moles, more preferably from about 3 to about 15 moles/ of ethylene oxide per mole of alkyl phenol. Commercially available nonionic surfactants of this type include Ideal™ CO-630, marketed by rhe GAF Corporation; and Triton X-45, X-114, X-IGO and X-102, all marketed by the Rohm & Has Company. These surfactants are commonly referred to as alkyl phenol alkoxylate e.g., alkyl phenol ethoxylated). The condensation products of primary and secondary aliphatic alcohols with about 1 to about 2 5 moles of ethylene oxide are suitable for use as the nonionic surfactant of the nonionic surfactant systems of the present invention. The alkyl cnalr. of the aliphatic alcohol can either be straight or ranched, primary or secondary, and generally contains from about S to about 22 carbon atoms. Preferred are the condensation products of alcohols having an alkyl- group containing from about S ~c about 20 carbon atoms, more preferably from about 10 to abcur 18 carbon atoms, with from about 2 to about 10 moles of s::hylene oxide per mole of alcohol. About 2 to moles of ethylene oxide and most preferably from 2 to 5 moils of ethylene oxide per mole of alcohol are present in said condensation pro-ours. Examples of commercially available nonionic surfactants of has type include Tergitol" 15-S-9 (The condensation product cN linear alcohol with 9 moles ethylene oxide) , Tergitol 24-L-6 NMW (the condensation product of C12-C14 primary alcohol wish 6 moles" ethylene oxide with a narrow molecular weight distribution}, both marketed by Union Carbide Corporation; Nodal" 45-9 (the condensation product of C14-C15 linear alcohol Ail 9 moles of ethylene oxide) , Nodal™ 2 3-3 (the condensation product of C12-C15 linear alcohol- with 3.0 moles of ethylene oxide) , ■Neod-ci™-~45--7 (the condensation product of C14-C15 linear-' alcohol "cithc 7 moles of ethylene oxide), Nodal'"" 45-5' (the condensation product of C24-C15 linear alcohol with 5 moles of ethylene oxide) marketed by Shell Chemical Company, Kino EOB [tie condensation product of with 5 maces ethylene oxide), marketed by The Procter 5 Gamble Company, and Glenpool LA 050 (~he condensation product of Civic- alcohol with 5 moles of ethylene oxide) marketed by Hoechst. Preferred range of HLB in these produces is fore 6-11 Ana nicer preferred from. 8- Also useful as the nonionic surfactant of the surfactant systems of the present invention are alkylpolysaccharides disclosed in US 4,565/647, having a hydrophobic group containing freer: about 6 to about 30 carbon atoms, preferably from about 10 is about 16 carbon atoms and a polysaccharide, e.g. a , hydrophilic group containing from about 1.3 to abacus 10, preferably from about 1.3 to about 3, most preferably fro-;: abcur 1.3 to about 2.7 saccharine units. Any reducing saccharine containing 5 or 6 carbon atoms can be used, e.g., glucose, galactose and galactose- moieties can be substituted for "crew glucosyl moieties 'optionally the hydrophobic group is ai*ached at the 2~, 3-, 4-, etc. positions thus giving a glucose or galactose as opposed to a glycoside or galactose). The ir.rersaccharide bonds can be, e.g., between the one position of rhea a -divisional saccharine curios and the 2-, 3-, 4-, and/or 6-posi ions on the preceding saccharine units. The preferred alkylpolyglycosides have the formula The additional glycidyl units can then be attached between their 1-pc5i~ion and the preceding glycidyl units 2-, 3-, 4-, and/or 6-position, preferably predominantly the 2-positicn. The condensation products of ethylene oxide with a Product contains from about 40% to about 8 0% by weight of pclyoxyethylene and has a molecular weight of from, about 5,000 ice about 11,000. Examples of this type of nonionic surfactant in" :-due certain of the commerce ally available Tectonic"""' compounds, marketed by BASF. Preferred for use as the nonionic surfactant of the surfactant systems - -the present invention are polyethylene oxide condensates of alkyl phenols, condensation products of primary and secondary aliphatic alcohols with from about 1 to abut 2 5 moles of ethylene oxide, alkylpolysacchariaes, and mixtures hereof. MgCIs. preferred are , alkyl phenol ethoxylated having from. 3 to 15 ethoxy groups and alcohol ethoxylated (preferably .) having from 2 cut 1C ethoxy contains an xyloglucanase activity. This xyloglucanase is incorporated into the cleaning compositions in accordance with the invention preferably at a level of fort: ::.GCC1% to 2%, more preferably frown 0.0005% to 0.5%, zincs preferred from 0.001% too. 1 % pure enzvTTie by weight of the composition. Preferred xyloglucanases for specific applications are alkaline xyloglucanases, ie enzymes having an enzymatic activity cN at leas- 10%, preferably at least 25%, more preferably at leas' 4 0% of "heir maximum activity at a pH ranging from 7 to 12. Mere preferred xyloglucanases are enzymes having their maxim it: activity at a pH ranging from 7 to 12. The above-mentioned enzymes may be of any suitable origin, such as vegetable, abnormal, bacterial, fungal and yeast origin. Origin can further be hemophilic or extremophilic (psychro-philic, psychotropic, thermopile, barophilic, alkalophilic, acidophilus, halophytic, etc.). Purified or non-purified forms fC ~hose enzyir:es may be used. Nowadays, it is common practice to modify wild-type enzymes via protein / genetic engineering techniques in order to optimize their performance efficiency in the cleaning compositions of the invention. For example, the variants may be designed such that the compatibility of the enzyme to commonly encountered ingredients of such compositions is increased. Alternatively, the variant may be designed such that ten optimal pH, bleach or Chelan stability, catalytic activity and the like, of the enzyme variant is tailored to suit the particular cleaning application. In particular, attention should be focused on amino acids sensitive to oxidation in the case of bleach stability and on surface charges for the surfactant compatibility. The is electric point of such enzymes may be modified by the substitution of some charged amino acids, e.g. an increase in bioelectric point may help to improve compatibility with anionic surfactants - The liability of he enzymes may be further enhanced by ~new creation of e.g. additional salt bridges and enforcing metal binding sites to increase Chelan stability. WE CLAIM: 1. An isolated mannanase which is (a) a polypeptide encodable by the mannanase enzyme encoding part of the DNA sequence cloned into the plasmid present in Escherichia coli DSM 12441, or (b) a polypeptide comprising an amino acid sequence as shown in positions 31-330 of SEQIDNO:12,or (c) a polypeptide encodable by the DNA sequence as shown in positions 97-993 of SEQIDNO:ll,or (d) an analogue of the polypeptide defined in (a) or (b) which is at least 85% homologous with said polypeptide, or a fragment of (a), (b) or (c). 2. The mannanase according to claim 1 which is derivable from a strain of Bacillus sp. 3. The mannanase according to claim 2 which has i) a relative mannanase activity of at least 50% in the pH range 7.5-10, measured at 40°C; ii) a molecular weight of 34 kDa, as determined by SDS-PAGE; and/or iii) the N-terminal sequence AHHSGFHVNGTTLYDA. 4. An isolated polynucleotide molecule comprising a DNA sequence encoding an enzyme exhibiting mannanase activity, which DNA sequence comprises: (a) the mannanase encoding part of the DNA sequence cloned into the plasmid present in Escherichia coli DSM 12441; (b) the DNA sequence shown in positions 97-993 in SEQ ID NO 11, or its complementary strand; (c) an analogue of the DNA sequence defined in (a) or (b) which is at least 85% homologous with said DNA sequence; (d) a DNA sequence which hybridizes with a double-stranded DNA probe comprising the sequence shown in positions 97-993 in SEQ ID NO 11 at medium stringency; (e) a DNA sequence which, because of the degeneracy of the genetic code, does not hybridize with the sequences of (b) or (d), but which codes for a polypeptide having exactly the same amino acid sequence as the polypeptide encoded by any of these DNA sequences; or a DNA sequence which is a fragment of the DNA sequences specified in (a), (b), (c), (d), or (e). 5. The cloned DNA sequence according to claim 4, in which the DNA sequence encoding an enzyme exhibiting mannanase activity is obtained from a microorganism, preferably a filamentous fungus, a yeast, or a bacteria; preferably from Bacillus, Caldicellulosiruptor or Hum cola. 6. An isolated polynucleotide molecule encoding a polypeptide having mannanase activity which polynucleotide molecule hybridizes to a denatured double-stranded DNA probe under medium stringency conditions, wherein the probe is selected from the group consisting of DNA probes comprising the sequence shown in positions 97-993 of SEQ ID NO: 11, and DNA probes comprising a subsequence of positions 97-993 of SEQ ID NO: 11 having a length of at least about 100 base pairs. 7. An expression vector comprising the following operably linked elements: a transcription promoter; a DNA segment selected from the group consisting of (a) polynucleotide molecules encoding a polypeptide having marmanase activity comprising a nucleotide sequence as shown in SEQ ID NO: 11 from nucleotide 97 to nucleotide 993, (b) polynucleotide molecules encoding a polypeptide having mannanase activity that is at least 85% identical to the amino acid sequence of SEQ ID NO: 12 from amino acid residue 31 to amino acid residue 330, and (c) degenerate nucleotide sequences of (a) or (b); and a transcription terminator. 8. A cultured cell, selected from a bacterial or fungal cell, into which has been introduced an expression vector according to claim 7, wherein said cell expresses the polypeptide encoded by the DNA segment. 9. An isolated polypeptide having mannanase activity selected from the group consisting of: (a) polypeptide molecules comprising an amino acid sequence as shown in SEQ ID NO: 12 from residue 31 to residue 330; and (b) polypeptide molecules that are at least 85% identical to the amino acids of SEQ ID NO: 12 from amino acid residue 31 to amino acid residue 330. 10. The polypeptide according to claim 9 which is produced by Bacillus holothurians. 11. An enzyme preparation comprising a purified polypeptide according to claim 9. 12. A method of producing a polypeptide having mannanase activity comprising culturing a cell into which has been introduced an expression vector according to claim 7, whereby said cell expresses a polypeptide encoded by the DNA segment; and recovering the polypeptide. 13. The preparation according to claim 11 which further comprises one or more enzymes selected from the group consisting of proteases, cellulases (endoglucanases), p-glutamates, hemicelluloses, lipases, peroxides, lactases, a-amylases, glucoamylases, cutinases, peptidases, reductase, oxidizes, phenoloxidases, clinginess, puUulanases, petite leases, xyloglucanases, cyanoses, pectin acetyl esterase’s. polygalacturonases, rhamnogalacturonases, pectin leases, other manganese’s, pectin methylesterases, cellobiohydrolases, transglutaminases; or mixtures thereof 14. An isolated enzyme having mannanase activity, in which the enzyme is (i) free from homologous impurities, and (ii) produced by the method according to claim 12. 15. A method for improving the properties of cellulosic or synthetic fibres, yam, woven or non-woven fabric in which method the fibres, yam or fabric is treated with an effective amount of the preparation according to claim 11 or an effective amount of the enzyme according to claim 1 or 2. 16. The method according to claim 15, wherein the enzyme preparation or the enzyme is used in a desisting process step. 17. A method for degradation or modification of plant material in which method the plant material is treated with an effective amount of the preparation according to claim 11 or an effective amount of the enzyme according to claim 1 or 2. 18. The method according to claim 17 wherein the plant material is recycled waste paper; mechanical, chemical, semi chemical, Kraft or other paper-making pulps; fibres subjected to a retting process; or guar gum or locust bean gum containing material. 19. A method for processing liquid coffee extract, in which method the coffee extract is treated with an effective amount of the preparation according to claim 11 or an effective amount of the enzyme according to claim 1 or 2. 20. A cleaning composition comprising the enzyme preparation according to claim 11 or the enzyme according to claim 1 or 2. 21. The cleaning composition according to claim 20 which further comprises an enzyme selected from cellulases, proteases, lipases, amylases, pectin degrading enzymes and xyloglucanases; and conventional detergent ingredient. 22. The cleaning composition according to claim 20 wherein said enzyme or enzyme preparation is present at a level of from 0.0001% to 2%, preferably from 0.0005% to 0.5%, more preferably from 0.001% to 0.1% pure enzyme by weight of total composition. 23. The cleaning composition according to claim 21 wherein the enzyme is present at a level of from 0.0001% to 2%, preferably from 0.0005% to 0.5%, more preferably from 0.001% to 0.1% pure enzyme by weight of total composition. 24. The cleaning composition according to claim 21 wherein the enzyme is an amylase. 25. The cleaning composition according to claim 24 which further comprises yet another enzyme selected from cellulases, protease, lipase, pectin degrading enzyme and xyloglucanase. 26. The cleaning composition according to claim 21 which comprises a surfactant selected from anionic, nonionic, cationic surfactant, and/or mixtures thereof. 27. The cleaning composition according to claim 21 which comprises a bleaching agent. 28. The cleaning composition according to claim 21 which comprises a builder. 29. A fabric softening composition according to claim 21 which comprises a cationic surfactant comprising two long chain lengths. 30. A process for machine treatment of fabrics which process comprises treating fabric during a washing cycle of a machine washing process with a washing solution containing the enzyme preparation according to claim 11 or the enzyme according to claim 1 or 2. 31. A method for removing stains on a fabric in which method the fabric is treated with an effective amount of an enzyme preparation according to claim 11 or the enzyme according to claim 1 or 2 together with a enzyme selected from cellulases, protease, lipase, amylase, pectin degrading enzyme and xyloglucanase. 32. A method for cleaning hard surfaces such as floors, walls, bathroom tile, dishes in which method the fabric is treated with an effective amount of an enzyme preparation according to claim 11 or the enzyme according to claim 1 or 2 together with a enzyme selected from cellulases, amylase, protease, lipase, pectin degrading enzyme and xyloglucanase.

Documents:

5237-CHENP-2007 AMENDED CLAIMS 08-11-2011.pdf

5237-CHENP-2007 AMENDED PAGES OF SPECIFICATION 08-11-2011.pdf

5237-chenp-2007 correspondence others 02-02-2011.pdf

5237-CHENP-2007 EXAMINATION REPORT REPLY RECEIVED 08-11-2011.pdf

5237-CHENP-2007 FORM-3 08-11-2011.pdf

5237-CHENP-2007 OTHER PATENT DOCUMENT 08-11-2011.pdf

5237-CHENP-2007 POWER OF ATTORNEY 08-11-2011.pdf

5237-chenp-2007-abstract.pdf

5237-chenp-2007-assignement.pdf

5237-chenp-2007-claims.pdf

5237-chenp-2007-correspondnece-others.pdf

5237-chenp-2007-description(complete).pdf

5237-chenp-2007-drawings.pdf

5237-chenp-2007-form 1.pdf

5237-chenp-2007-form 26.pdf

5237-chenp-2007-form 3.pdf

5237-chenp-2007-form 5.pdf