A cellulase preparation useful for reducing the harshness of cotton-containing fabrics and for reducing the rate at which such fabrics become harsh comprises about 40% or more (based on the total protein content) of an endoglucanase component with a pH optimum of about 7.5-10.0 with a high CMC-endoase activity and affinity towards cellulose and essentially no cellobiohydrolase activity. The cellulase composition is endogenous to a strain of Humicola, Myceliophthora, or Fusarium.

Fungal cellulase composition containing alkaline CMC-endoglucanase and essentially no cellobiohydrolase

Depolymerization of cellulose to glucose requires the synergistic action of three key cellulases, endoglucanase (E.C. 3.2.1.4), exoglucanase (E.C. 3.2.1.176) (E.C. 3.2.1.91) and β-glucosidase (E.C. 3.2.1.21). They belong to the glycoside hydrolase (GH) family and catalyze the hydrolysis of glyosidic linkages depolymerizing cellulose to fermentable sugars. Cellulases are naturally produced by a wide spectrum of bacteria and fungi. These enzymes usually exist as cellulosomes attached to the cell wall of bacteria but are secreted into environments in fungi. They exist either as monomers or multimers with each monomer having a simple architecture containing a cellulose binding domain (CBD) and a catalytic domain (CD) interlinked by a linker peptide. Thermophilic, mesophilic and psychrophilic cellulases are quite different in their structures and amino acid compositions. Post-translational modifications such as glycosylation contribute to enzyme function, multiplicity and stability. Recent advances in recombinant DNA technology allow fast identification of novel cellulase genes, large scale production of cellulases and their genetic modifications to make tailor-made enzymes for various applications. Cellulases have been traditionally used in food processing and textile industries. The rapid depletion of fossil fuels and production of cheap fermentable sugars from abundant renewable resources have increased the demand for cellulases in lignocellulose-based biorefinery. However, the lack of a better understanding of the mechanisms of individual cellulases, their synergistic actions and their high prices are the major bottlenecks yet to be overcome for large scale commercial applications of cellulases in lignocellulose-based biorefinery.

Microbial cellulases: Engineering, production and applications

The present invention relates to isolated polypeptides having cellulolytic enhancing activity and isolated polynucleotides encoding the polypeptides. 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.

Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same

Cellulases selected from the group consisting of Family 7 cellulases and variants of these cellulases comprising a core and optionally a C-terminal link consisting of 10 amino acids at the most, especially cellulases having tryptophan, tyrosine or phenylalanine in position 55 relative to the sequence alignment of Figure 5 and/or cellulases having a substrate binding cleft of a depth of at least 12 A, exhibit enhanced enzyme activity in the alkaline pH range while exerting a moderate cellulolytic action on the cellulosic substrate and are, for example, useful in detergent compositions, especially for soil removal or colour clarification or preventing backstaining; in fabric softeners; for bio-polishing of textiles; for drainage improvement of paper pulp; for plant degradation. Cellulases from Humicola insolens, Fusarium oxysporum, Trichoderma reesei and Myceliophthora thermophile are referred to.

Novel alkaline cellulases

Enzymatic surface modification of poly(ethylene terephthalate)

Disclosed are cellulase compositions containing one or more endoglucanase components and less than about 5 weight percent of CBH I type components. When incorporated into detergent compositions and used in acidic, neutral, or alkaline washing media, such cellulase compositions impart rotor retention/restoration properties as well as improved softening properties to cotton-containing fabrics. Additionally, such compositions impart reduced strength loss to cotton-containing fabrics as compared to cellulase compositions containing greater amounts of CBH I type components.

Detergent compositions containing cellulase compositions deficient in cbh i type components

Disclosed are improved methods for treating cotton-containing fabrics as well as the fabrics produced from these methods. In particular, the disclosed methods are directed to contacting cotton-containing fabrics with a cellulase solution containing a fungal cellulase composition which is substantially free of all CBH I type cellulase components. Cotton-containing fabrics so treated possess decreased strength loss as compared to fabrics treated with a cellulase solution containing a complete cellulase composition.

Method for treating cotton-containing fabric with a cellulase composition containing endoglucanase components and which composition is free of exo-cellobiohydrolase I

A method for treating cellulosic materials is disclosed which comprises contacting the cellulosic material with a cellulase obtainable from Thermomonospora fusca corresponding to E5 or a derivative thereof. Particularly preferred methods comprise stonewashing and detergent cleaning of cotton fabrics, the production of paper products, as an additive to animal feed and in the production of food, starch, ethanol and sugar.

Cellulase obtainable from thermomonospora fusca for use in industrial processes

The present invention is directed to purified EG III cellulase enzyme isolated from Trichoderma longibrachiatum and the amino acid sequence of the secreted (mature) and non-secreted (preprotein) forms. The present invention is further directed to the DNA fragment and sequence that encodes the EG III cellulase enzyme. Also disclosed are methods for isolating either purified or highly enriched EG III cellulase obtained from Trichoderma spp. or genetically modified strains of Trichoderma spp.

Kathleen A. Clarkson

Papers

Detergent compositions containing cellulase compositions deficient in cbh i type components

Method for treating cotton-containing fabric with a cellulase composition containing endoglucanase components and which composition is free of exo-cellobiohydrolase I

Cellulase obtainable from thermomonospora fusca for use in industrial processes

DNA sequence encoding endoglucanase III cellulase

Methods for treating cotton-containing fabrics with cellulase