C12Y302/01055

Arabinanase and uses thereof

The invention relates to the use of an isolated arabinanase enzyme comprising the activities of (1-5)--arabinofuranosidic linkage endohydrolysis in (1-5)--L-arabinans (EC 3.2.1.99), and hydrolysis of (1-5)--arabinofuranosidic linkages at the non-reducing end of -L-arabinans or -L-arabinose-oligomers (EC 3.2.1.55), particularly an arabinan-degrading enzyme isolated from Arxula adeninivorans as feed additive in livestock breeding. Furthermore, the invention relates to the application of the arabinanase in the production of fruit juices or biofuels.

POLYPEPTIDES HAVING XYLANASE ACTIVITY AND POLYNUCLEOTIDES ENCODING SAME

The present invention relates to polypeptides having xylanase activity and 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. The invention also relates to compositions comprising the polypeptides of the invention and the use of the polypeptides of the invention to release xylose and in animal feed.

Polypeptides having xylanase activity and polynucleotides encoding same

The present invention relates to polypeptides having xylanase activity and 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. The invention also relates to compositions comprising the polypeptides of the invention and the use of the polypeptides of the invention to release xylose and in animal feed.

Compositions Comprising Polypeptides Having Xylanase Activity and Polypeptides Having Arabinofuranosidase Activity

The present invention relates to compositions comprising polypeptides having xylanase activity and polypeptides having arabinofuranosidase activity for use in, e.g., animal feed. The present invention further relates to polypeptides having arabinofuranosidase activity, polypeptides having xylanase activity and 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.

Compositions comprising polypeptides having xylanase activity and polypeptides having arabinofuranosidase activity

Compositions comprising polypeptides having xylanase activity and polypeptides having arabinofuranosidase activity for use in e.g. animal feed. Polypeptides having arabinofuranosidase activity, polypeptides having xylanase activity and polynucleotides encoding the polypeptides. Nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptide.

METHOD FOR PREPARATION AND SCREENING OF FUNGAL MUTANT WITH HIGH HYDROLYTIC ACTIVITY AND CATABOLITE DEREPRESSED CHARACTER

The present invention relates to a mutant fungal strain of Penicillium funiculosum MRJ-16 characterized by the ability to produce high titer of enzyme mixture comprising FPase, CMCase, Cellobiase, -glucosidase, endoglucanase, -L arabinofuranosidase, -xylosidase, xylanase, pectinase, cellobiohydrase and oxidases and produce enzymes in the presence of a catabolite repressor molecule like glucose and/or xylose. The titer of enzyme mixture produced using mutant fungal strain MRJ-16 is at least two fold higher than naive Penicillium funiculosum strain NCIM 1228, when used in a fermentation process. The mutant strain MRJ-16 with high hydrolytic activity and catabolite derepressed character is having application in the method of degrading or saccharifying biomass to produce valuable products for example-bioethanol.

Thermophilic and thermoacidophilic biopolymer-degrading genes and enzymes from Alicyclobacillus acidocaldarius and related organisms, methods

Isolated and/or purified polypeptides and nucleic acid sequences encoding polypeptides from Alicyclobacillus acidocaldarius are provided. Further provided are methods of at least partially degrading, cleaving, or removing polysaccharides, lignocellulose, cellulose, hemicellulose, lignin, starch, chitin, polyhydroxybutyrate, heteroxylans, glycosides, xylan-, glucan-, galactan-, or mannan-decorating groups using isolated and/or purified polypeptides and nucleic acid sequences encoding polypeptides from Alicyclobacillus acidocaldarius.

Polypeptides having arabinofuranosidase activity and polynucleotides encoding same

The present invention relates to isolated polypeptides having arabinofuranosidase activity, catalytic domains, carbohydrate binding modules and polynucleotides encoding the polypeptides, catalytic domains or 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 or carbohydrate binding modules.

Method for obtaining a composition for biomass hydrolysis

The present invention discloses a composition for biomass hydrolysis. The components of the composition may be obtained by biological or synthetic means. Synthetically, the components of the composition of the present invention may be obtained by amino acid synthesis or may be procured commercially.

Analytical method for determining the concentration of oxidized nanofibrillar cellulose in a sample

The present invention provides a method for determining carbonyl ratio and/or concentration of oxidized nanofibrillar cellulose in a sample. In accordance with the invention oxidized nanofibrillar cellulose comprised in the sample is enzymatically hydrolyzed into oxidized cellobioses which are specific markers to oxidized nanofibrillar cellulose. The cellobioses may be then analyzed and quantified to reveal the amount of oxidized nanofibrillar cellulose in the sample. A method for determining the concentration of oxidized nanofibrillar cellulose in a sample comprises steps of providing an analytical sample of material comprising oxidized nanofibrillar cellulose; hydrolyzing the analytical sample to breakdown products of oxidized nanofibrillar cellulose in presence of one or more enzymes; subjecting the breakdown products to a separation analysis to reveal the relative amounts of the breakdown products; and determining the concentration of oxidized nanofibrillar cellu-lose.