Abstract: A high temperature resistant mannanase mutant, comprising at least one mutation site among D49C/I/N, G58D/E/S, H90L, T99Y, K120Y, N124P, T130D/N/P/Q/R/S, Y132F, S136M, S140L/K, T148K, F206Y, A212N/S/P, L257F, S263R, D268A/E/G/P, G273P, S302M/E, S306M/Q, T315P, T353L/F, D360E/N/K, and A362R. The high temperature resistant mannanase mutant has heat resistance significantly higher than the wild type mannanase, and can be widely used in the field of feeds.

Abstract: Provided is a method for producing washing enzyme having protease resistance. According to the method, the washing enzyme having resistance to protease is obtained by carrying out fusion expression on a gene of the washing enzyme with the gene of a protease inhibitory peptide, thereby facilitating maintaining the stability of various enzyme components in an enzyme-containing detergent, and improving the use effect of the detergent.

Abstract: Provided are a Bacillus coagulans strain VHProbi C08 having a blood glucose reduction efficacy and an application thereof in preparation of a hypoglycemic product. The accession number of the strain is CCTCCM 2019738. Further provided is a hypoglycemic product comprising the Bacillus coagulans VHProbi C08 and/or the fermentation product of Bacillus coagulans VHProbi C08. A carbon source used in the culture medium of the strain is any one or more of fructooligosaccharide, galactooligosaccharides, and inulin.

Abstract: Provided are mutants PHY1, PHY4 and PHY5 of a wild-type phytase APPA. After being treated for 10 min at 80° C., the residual enzyme activities of the mutants PHY1, PHY4 and PHY5 are respectively higher by 33.85%, 53.11% and 75.86% compared with that of APPA-M; after being treated for 5 min at 85° C., the residual enzyme activities of the mutants PHY1, PHY4 and PHY5 are respectively higher by 14.89%, 28.45% and 44.94% compared with that of APPA-M, and the heat resistance of these mutants is significantly higher than that of APPA-M.

Abstract: Provided are a phytase mutant and a coding DNA molecule thereof, a vector, and a host cell. The phytase mutant comprises an amino acid sequence having at least 90% identity with SEQ ID NO: 3, and compared with SEQ ID NO: 3, and contains an amino acid substitution at at least one position selected from the group consisting of 36, 126, 211, 253, 258, and 266. The heat resistance of the mutant is significantly improved, thus facilitating the wide application of phytase in feed.

Abstract: Provided is a xylanase mutant having improved specific activity, comprising any one or more mutation sites of M78F, V1431, R148K, F163W, I177V, and V206L. The specific activity of the mutant is improved, the production cost of xylanase is reduced, and the mutant can be used in feed.

Abstract: The present invention relates to the technical field of biology, in particular to a phytase mutant, a preparation method therefor and an application thereof, a DNA molecule encoding the phytase mutant, a vector, and a host cell. The mutant provided by the present invention contains the substituent of an amino acid at at least one position selected from the following group: 36, 69, 89, 91, 111, 202, 213, 225, 238, 243, 253, 258, and 266. The heat resistance of the mutant is significantly improved, thereby facilitating the wide application of the phytase in feed.

Abstract: Provided is a method for producing washing enzyme having protease resistance. According to the method, the washing enzyme having resistance to protease is obtained by carrying out fusion expression on a gene of the washing enzyme with the gene of a protease inhibitory peptide, thereby facilitating maintaining the stability of various enzyme components in an enzyme-containing detergent, and improving the use effect of the detergent.

Abstract: Provided are phytase mutants, preparation methods therefor and uses thereof, DNA molecule encoding each of the phytase mutants, a vector comprising the DNA molecule, and a host cell comprising the vector.

Abstract: Provided are mutants PHY1, PHY4 and PHY5 of a wild-type phytase APPA. After being treated for 10 min at 80° C., the residual enzyme activities of the mutants PHY1, PHY4 and PHY5 are respectively higher by 33.85%, 53.11% and 75.86% compared with that of APPA-M; after being treated for 5 min at 85° C., the residual enzyme activities of the mutants PHY1, PHY4 and PHY5 are respectively higher by 14.89%, 28.45% and 44.94% compared with that of APPA-M, and the heat resistance of these mutants is significantly higher than that of APPA-M.

Abstract: The present invention relates to the technical field of protein engineering, and, in particular, to a xylanase mutant with improved heat tolerance. The present invention artificially introduces two or three unnatural disulfide bridges into xylanase by site-directed mutagenesis and obtains the mutants XynA1 and XynA2 with improved heat tolerance, especially the mutant XynA2 into which three disulfide bridges are introduced, achieving residual enzyme activity of 75% after treatment at 80° C. for 5 min, 72% higher than the residual enzyme activity of the mutant XynA1. The present invention further obtains, by screening, three mutation sites Q51N, H143K, and Q161F that can significantly increase the heat tolerance of mutants, and introduction of the mutation sites into the XynA1 and XynA2 xylanases, whether at a single point or a combination of two points or a combination of three points, can effectively improve the heat tolerance of the mutants.

Abstract: The present invention relates to the technical field of protein engineering, and, in particular, to a xylanase mutant with improved heat tolerance. The present invention artificially introduces two or three unnatural disulfide bridges into xylanase by site-directed mutagenesis and obtains the mutants XynA1 and XynA2 with improved heat tolerance, especially the mutant XynA2 into which three disulfide bridges are introduced, achieving residual enzyme activity of 75% after treatment at 80° C. for 5 min, 72% higher than the residual enzyme activity of the mutant XynA1. The present invention further obtains, by screening, three mutation sites Q51N, H143K, and Q161F that can significantly increase the heat tolerance of mutants, and introduction of the mutation sites into the XynA1 and XynA2 xylanases, whether at a single point or a combination of two points or a combination of three points, can effectively improve the heat tolerance of the mutants.

Abstract: The invention provides novel carbohydrate esters, in particular disaccharide esters, and the methods of their preparation. These compounds find use as microbial media components for the induction of gene expression in microbial fermentation processes.

Abstract: The present disclosure provides a sophorolipid composition that can be used for inducing protein expression in a fermentation host. The sophorolipid composition described herein can be prepared from a natural sophorolipid mixture. Acid treatment of the natural sophorolipid mixture results in a mixture of monoacetylated, deacetylated, and/or diacetylated sophorolipids. The chemically modified sophorolipid composition, or isolated components of the chemically modified sophorolipid composition, can be used as inducers for protein production in filamentous fungi.