A23K10/14

POLYPEPTIDE FOR HYDROLYTIC CLEAVAGE OF ZEARALENONE AND/OR ZEARALENONE DERIVATIVES, ISOLATED POLYNUCLEOTIDE THEREOF AS WELL AS A POLYPEPTIDE CONTAINING AN ADDITIVE, USE OF SAME AS WELL AS A PROCESS

The invention relates to a polypeptide for the hydrolytic cleavage of zearalenone and/or at least one zearalenone derivative, said polypeptide being a hydrolase having an amino acid sequence selected from the group consisting of SEQ ID NO: 1-15 or a functional variant thereof, wherein the sequence of the functional variant is at least 40% identical to at least one of the amino acid sequences. The invention also relates to: an additive containing the polypeptide; an isolated polynucleotide that encodes the polypeptide; and a method for the hydrolytic cleavage of zearalenone and/or of at least one zearalenone derivative using the polypeptide.

POLYPEPTIDE FOR HYDROLYTIC CLEAVAGE OF ZEARALENONE AND/OR ZEARALENONE DERIVATIVES, ISOLATED POLYNUCLEOTIDE THEREOF AS WELL AS A POLYPEPTIDE CONTAINING AN ADDITIVE, USE OF SAME AS WELL AS A PROCESS

The invention relates to a polypeptide for the hydrolytic cleavage of zearalenone and/or at least one zearalenone derivative, said polypeptide being a hydrolase having an amino acid sequence selected from the group consisting of SEQ ID NO: 1-15 or a functional variant thereof, wherein the sequence of the functional variant is at least 40% identical to at least one of the amino acid sequences. The invention also relates to: an additive containing the polypeptide; an isolated polynucleotide that encodes the polypeptide; and a method for the hydrolytic cleavage of zearalenone and/or of at least one zearalenone derivative using the polypeptide.

POLYPEPTIDE FOR HYDROLYTIC CLEAVAGE OF ZEARALENONE AND/OR ZEARALENONE DERIVATIVES, ISOLATED POLYNUCLEOTIDE THEREOF AS WELL AS A POLYPEPTIDE CONTAINING AN ADDITIVE, USE OF SAME AS WELL AS A PROCESS

The invention relates to a polypeptide for the hydrolytic cleavage of zearalenone and/or at least one zearalenone derivative, said polypeptide being a hydrolase having an amino acid sequence selected from the group consisting of SEQ ID NO: 1-15 or a functional variant thereof, wherein the sequence of the functional variant is at least 40% identical to at least one of the amino acid sequences. The invention also relates to: an additive containing the polypeptide; an isolated polynucleotide that encodes the polypeptide; and a method for the hydrolytic cleavage of zearalenone and/or of at least one zearalenone derivative using the polypeptide.

POLYPEPTIDE FOR HYDROLYTIC CLEAVAGE OF ZEARALENONE AND/OR ZEARALENONE DERIVATIVES, ISOLATED POLYNUCLEOTIDE THEREOF AS WELL AS A POLYPEPTIDE CONTAINING AN ADDITIVE, USE OF SAME AS WELL AS A PROCESS

The invention relates to a polypeptide for the hydrolytic cleavage of zearalenone and/or at least one zearalenone derivative, said polypeptide being a hydrolase having an amino acid sequence selected from the group consisting of SEQ ID NO: 1-15 or a functional variant thereof, wherein the sequence of the functional variant is at least 40% identical to at least one of the amino acid sequences. The invention also relates to: an additive containing the polypeptide; an isolated polynucleotide that encodes the polypeptide; and a method for the hydrolytic cleavage of zearalenone and/or of at least one zearalenone derivative using the polypeptide.

LOW LIPID CONTENT OAT PROTEIN COMPOSITION WITHOUT TRACES OF ORGANIC SOLVENT
20220240540 · 2022-08-04 ·

The invention pertains to the field of oat protein compositions and production method thereof. In particular, the present invention is directed to an oat protein composition having low lipid content and which does not contain traces of organic solvent and to the production method thereof.

DIGESTION OF FORAGE CONTAINING LIGNOCELLULOSE WITH FIBROLYTIC ENZYMES AND RECOMBINANT BACTERIAL EXPANSINS

Studies on a recombinant bacterial expansin-like protein from Bacillus subtilis (BsEXLXt) and a commercial exogenous fibrolytic enzyme (EFE) preparation for ruminants on the hydrolysis of pure substrates (cellulose and xylan) and in vitro digestibility of bermudagrass haylage have shown that, compared to EFE alone, EFE and BsEXLXt synergistically increased sugar release from carboxymethylcellulose and filter paper. Therefore, a combination of EFE and an expansin-like protein is useful to improve the hydrolysis of cellulose-containing substrates and the hydrolysis and digestibility of forage in vitro.

DIGESTION OF FORAGE CONTAINING LIGNOCELLULOSE WITH FIBROLYTIC ENZYMES AND RECOMBINANT BACTERIAL EXPANSINS

Studies on a recombinant bacterial expansin-like protein from Bacillus subtilis (BsEXLXt) and a commercial exogenous fibrolytic enzyme (EFE) preparation for ruminants on the hydrolysis of pure substrates (cellulose and xylan) and in vitro digestibility of bermudagrass haylage have shown that, compared to EFE alone, EFE and BsEXLXt synergistically increased sugar release from carboxymethylcellulose and filter paper. Therefore, a combination of EFE and an expansin-like protein is useful to improve the hydrolysis of cellulose-containing substrates and the hydrolysis and digestibility of forage in vitro.

XYLANASE MUTANT AND ITS PREPARATION METHOD AND APPLICATION
20220251527 · 2022-08-11 ·

The present invention discloses a kind of xylanase mutant and its preparation method and application, which relates to the technical field of genomic engineering and genetic engineering. Such mutant includes one or more mutants obtained by taking xylanase HwXyl10A as female parent to conduct saturation mutagenesis to the site of Gly363. Specifically, relates to obtaining 19 mutants through site-directed mutagenesis, and then conducting yeast expression to them, after that, obtaining two mutants with significantly improved specific activity and thermal stability through screening of thermal stability and catalytic activity; the present invention can significantly improve the thermal stability and catalytic efficiency of xylanase through modifying the site of Gly363, and is of important guiding significance for improving the thermal stability and the catalytic efficiency of the 10th family of xylanases and other glycoside hydrolases as well as lays the foundation for its application in industrial production.

Enzymatic degradation of mycotoxins during grain processing
11390832 · 2022-07-19 · ·

Methods, compositions, and systems for steeping, propagation and fermentation, particularly large-scale operations for production of starch and ethanol and fermentation product streams are provided. Addition of mycotoxin mitigating enzymes or microorganisms expressing mycotoxin mitigating enzymes to steeping, propagation, and/or fermentation tanks, and/or to post-fermentation product streams, mitigates mycotoxin levels in fermentation co-products obtained from mycotoxin contaminated feedstocks.

Enzymatic degradation of mycotoxins during grain processing
11390832 · 2022-07-19 · ·

Methods, compositions, and systems for steeping, propagation and fermentation, particularly large-scale operations for production of starch and ethanol and fermentation product streams are provided. Addition of mycotoxin mitigating enzymes or microorganisms expressing mycotoxin mitigating enzymes to steeping, propagation, and/or fermentation tanks, and/or to post-fermentation product streams, mitigates mycotoxin levels in fermentation co-products obtained from mycotoxin contaminated feedstocks.