The present invention relates to polypeptides having mannanase activity, catalytic domains, and carbohydrate binding modules, and polynucleotides encoding the polypeptides, catalytic domains, and carbohydrate binding modules. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides, catalytic domains, and carbohydrate binding modules.

The present invention relates to polypeptides having mannanase activity, catalytic domains, and carbohydrate binding modules, and polynucleotides encoding the polypeptides, catalytic domains, and carbohydrate binding modules. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides, catalytic domains, and carbohydrate binding modules.

The current invention discloses enzyme-based compositions for converting raw natural fibres from plant derived biomass into high quality textile grade fibres. The invention discloses at least one multi-component enzymatic formulation, and the optimal conditions for using these enzymatic formulations, which result in production of textile grade fibres from raw natural fibres. These textile grade fibres can be used in any industry, because of their high-quality parameters, and high spinnability index.

The present invention relates to aqueous surfactant compositions, in particular detergents, which contain at least one catechol compound, at least one surfactant, and at least one mannanase enzyme. The present invention further relates to the use of the surfactant composition for removing bleachable stains and to a method for washing textiles using the surfactant composition.

Novel hyperthermophilic Dictyoglomus beta-mannanases are provided for use in high temperature industrial applications requiring enzymatic hydrolysis of 1,4-β-D-mannosidic linkages in mannans, galactomannans, and glucomannans. Also provided are methods and compositions for fracturing a subterranean formation in which a gellable fracturing fluid is first formed by blending together a hydratable polymer and a Dictyoglomus beta-mannanase as an enzyme breaker. An optimized and stabilized recombinant Dictyoglomus beta-mannanase is provided that shows superior performance/effectiveness and properties in degrading guar and derivatized guars at pH ranges from 3.0 to 12 and temperatures ranging from 130° F. to in excess of 270° F.

The present invention relates to a mannanase PMan5A mutant having improved heat resistance, a gene encoding the mutant and application thereof. The mutant is obtained by a substitution of histidine with tyrosine at amino acid residue 93, phenylalanine with tyrosine at amino acid residue 94, leucine with histidine at amino acid residue 356, and/or alanine with proline at amino acid residue 389. The thermal tolerance of the single site mutation mutant H93Y, L356H and A389P are greatly improved over that of the wild-type mannanase PMan5A, and the thermal tolerance of the combination mutants shows the stack effect of the single site mutation, demonstrating the amino acids at the sites of 93, 94, 356, and 389 play an important role for the thermal stability of the mannanase of GH5 family.

The present invention relates to a method of producing a recombinant polypeptide a filamentous fungus which is genetically modified to decrease or eliminate the activity of cellulase regulator 2 (CLR2) and to express said recombinant polypeptide. The method further relates to a filamentous fungus Myceliophthora thermophila, which is genetically modified to decrease or eliminate the activity of CLR2 and the use of this filamentous fungus in the production of a recombinant polypeptide.

The present invention relates to compositions such as cleaning compositions comprising a mix of enzymes. The invention further relates, use of compositions comprising such enzymes in cleaning processes.

The present invention relates to mannanase PMan5A mutant having improved heat resistance, gene and application thereof. Said mutant is obtained by substitution the 93.sup.th histidine with tyrosine, the 94.sup.th phenylalanine with tyrosine, the 356.sup.th leucine with histidine, and/or the 389.sup.th alanine with proline. The thermal tolerance of the single site mutation mutant H93Y, L356H and A389P are greatly improved over that of the wild mannanase PMan5A, and the thermal tolerance of the combination mutants shows the stack effect of the single site mutation, demonstrating the amino acids at the sites of 93, 94, 356, and 389 play the important role for the thermal stability of the mannanase of GH5 family

The present invention relates to mannanase variants. The present invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants.