Abstract: The present invention relates to the fields of microorgan-isms, feed, food and ecological restoration, in particular to a strain for degrading deoxynivalenol (DON) and the use thereof. The strain has the deposit number CCTCC No. M 2020565. The strain can grow by means of taking the toxic compound DON as a sole carbon source, and convert the DON into chemical components for itself. The reaction process is irreversible, the reaction conditions are moderate, and secondary pollu-tion cannot be caused. The strain provided in the present invention can be used for preparing a biological detoxification preparation for DON. The strain provided in the present invention can be used for degrading DON in feed and food raw materials, primary processing products, deep processing products and related processing byproducts. The strain provided in the present invention can be applied to various ecosystems such as soil or bodies of water polluted by DON to achieve the purposes of DON degradation and ecological restoration.

Abstract: The present invention relates to the field of genetic engineering, particularly to a glucose oxidase mutant having improved thermal stability, gene and application thereof. The present invention provides several glucose oxidase GOD mutants with high catalytic efficiency and improved thermal stability, which breaks the barrier of low enzyme activity and poor stability and is suited well to meet the requirements of application to the fields of food, medicine, feed and textile industry, and has a very broad application prospect.

Abstract: The present invention relates to the field of genetic engineering, particularly to a glucoamylase TIGa15, gene and application thereof. Said glucoamylase comprises the amino acid sequence of SEQ ID NO:1 or SEQ ID NO:2 and has the excellent enzymic properties, which can be applied to feed, food, and medicine industries, can be industrially produce with the genetic engineering technics.

Abstract: The present invention provides use of a manganese peroxidase in the detoxification of mycotoxins, and specifically, the present invention provides five manganese peroxidases (MnP-1, MnP-2, MnP-4, MnP-5, and MnP-6), genes thereof, and uses thereof. The present invention provides five manganese peroxidases (MnP-1, MnP-2, MnP-4, MnP-5, and MnP-6) derived from lignocellulose degradation bacteria, the amino acid sequences thereof being as set forth in SEQ ID NO: 1, SEQ ID NO: 4, SEQ ID NO: 7, SEQ ID NO: 10, and SEQ ID NO: 13.

Abstract: The present invention takes the glucose oxidase GOD from Aspergillus niger as the mutation template to obtain the glucose oxidase GOD mutants with improved catalytic efficiency and thermal stability by site directed mutagenesis. The specific activity of the mutant of the present invention is 66% higher than that of the wild type GOD; the enzyme activity of the mutant of the present invention is 13.6 times higher than that of the wild type after being treated at 70° C. for 10 min; and the enzyme activity of the mutant of the present invention is 29.4 times higher than that of the wild type after being treated at 80° C. for 2 min.

Abstract: 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.

Abstract: The present invention relates to the field of agriculture biotechnology, specially relates to an amylase mutant having high specific activity and thermal stability, gene and use thereof. Said amylase mutant is obtained by performing substitution of S33A/S34E/V35H, and deletion of amino acids at the sites of 178 and 179 of the wild type amylase having amino acid sequence of SEQ ID NO:1, and having improved enzymatic activity and thermal stability than the wild type amylase.

Abstract: The present invention relates to the field of genetic engineering, particularly to a recombinant expression vector for rapidly screening the high expression strains and a method for rapidly screening high expression strains. In the invention, an exogenous red fluorescent protein and Aspergillus fumigatus cell surface protein localization signal are fused and expressed, and the fusion gene (DsRed-AfMP1) is integrated into the genome of Trichoderma reesei, so as to construct a strain displaying red fluorescent protein on the surface of Trichoderma reesei. By sorting Trichoderma reesei strains with red fluorescent protein on the surface by flow cytometry, genes beneficial to the improvement of cellulase activity can be quickly isolated.

Abstract: The present invention relates to the field of genetic engineering, particularly to a glucoamylase TIGal5, gene and application thereof. Said glucoamylase comprises the amino acid sequence of SEQ ID NO:1 or SEQ ID NO:2 and has the excellent enzymic properties, which can be applied to feed, food, and medicine industries, can be industrially produce with the genetic engineering technics.

Abstract: The present invention takes the glucose oxidase GOD from Aspergillus niger as the mutation template to obtain the glucose oxidase GOD mutants with improved catalytic efficiency and thermal stability by site directed mutagenesis. The specific activity of the mutant of the present invention is 66% higher than that of the wild type GOD; the enzyme activity of the mutant of the present invention is 13.6 times higher than that of the wild type after being treated at 70° C. for 10 min; and the enzyme activity of the mutant of the present invention is 29.4 times higher than that of the wild type after being treated at 80° C. for 2 min.

Abstract: The present invention relates to mannanase PMan5A mutant having improved heat resistance, gene and application thereof. Said mutant is obtained by substitution the 93th histidine with tyrosine, the 94th phenylalanine with tyrosine, the 356th leucine with histidine, and/or the 389th alanine with proline.

Abstract: The present invention provides use of a manganese peroxidase in the detoxification of mycotoxins, and specifically, the present invention provides five manganese peroxidases (MnP-1, MnP-2, MnP-4, MnP-5, and MnP-6), genes thereof, and uses thereof. The present invention provides five manganese peroxidases (MnP-1, MnP-2, MnP-4, MnP-5, and MnP-6) derived from lignocellulose degradation bacteria, the amino acid sequences thereof being as set forth in SEQ ID NO: 1, SEQ ID NO: 4, SEQ ID NO: 7, SEQ ID NO: 10, and SEQ ID NO: 13.

Abstract: Provided are acidic thermophilic polygalacturonase TePG28A, encoding gene and application thereof. The amino acid sequence thereof is as shown in SEQ ID NO. 1 or SEQ ID NO. 2. The expressed acidic thermophilic polygalacturonase by means of cloning has advantages such as high enzyme activity and high stability; can adapt to the high temperature environment in the industrial production; has better application prospect; and can effectively degrade pectic substances such as polygalacturonic acid and pectin; and can be effectively applied to the industrial field of feed, food, and textile, etc.

Abstract: Provided are a glucose oxidase CnGODA, an encoding gene thereof, a recombinant expression vector comprising the gene, and a recombinant strain; the amino acid sequence of the glucose oxidase CnGODA is as represented in SEQ ID NO:1 or SEQ ID NO:2. Further provided is a method for use in preparing glucose oxidase CnGODA, and application of glucose oxidase CnGODA.

Abstract: The present invention relates to the field of agriculture biotechnology, specially relates to an amylase mutant having high specific activity and thermal stability, gene and use thereof. Said amylase mutant is obtained by performing substitution of S33A/S34E/V35H, and deletion of amino acids at the sites of 178 and 179 of the wild type amylase having amino acid sequence of SEQ ID NO:1, and having improved enzymatic activity and thermal stability than the wild type amylase.

Abstract: Provided are a fungus-sourced high-temperature neutral Family-45 cullulase as well as a coding gene and application thereof. The cullulase has optimal pH value of 5.5, and optimal temperature of 60° C., has certain enzyme activity in alkaline condition, and has good alkali resistance, maintains about 70% enzyme activity in optimal condition after being processed at 90° C. for 1 hour, maintains about 50% enzyme activity in optimal condition after being processed in boiling water for 1 hour, and can be well applied in c and other fields.

Abstract: Provided are acidic thermophilic polygalacturonase TePG28A, encoding gene and application thereof. The amino acid sequence thereof is as shown in SEQ ID NO. 1 or SEQ ID NO. 2. The expressed acidic thermophilic polygalacturonase by means of cloning has advantages such as high enzyme activity and high stability; can adapt to the high temperature environment in the industrial production; has better application prospect; and can effectively degrade pectic substances such as polygalacturonic acid and pectin; and can be effectively applied to the industrial field of feed, food, and textile, etc.

Abstract: Provided are a glucose oxidase CnGODA, an encoding gene thereof, a recombinant expression vector comprising the gene, and a recombinant strain; the amino acid sequence of the glucose oxidase CnGODA is as represented in SEQ ID NO.1 or SEQ ID NO.2. Further provided is a method for use in preparing glucose oxidase CnGODA, and application of glucose oxidase CnGODA.

Abstract: Provided are a fungus-sourced high-temperature neutral Family-45 cullulase as well as a coding gene and application thereof. The cullulase has optimal pH value of 5.5, and optimal temperature of 60° C., has certain enzyme activity in alkaline condition, and has good alkali resistance, maintains about 70% enzyme activity in optimal condition after being processed at 90° C. for 1 hour, maintains about 50% enzyme activity in optimal condition after being processed in boiling water for 1 hour, and can be well applied in c and other fields.

Abstract: Provided are a fungus-sourced high-temperature acid ?-glucosidase as well as a coding gene, and an application thereof. The provide ?-glucosidase has the optimal pH value of 4.5 and the optimal temperature of 75° C., and maintains over 90% enzyme activity in the optimal condition after being processed at 60° C. for 1 h. The re-engineering yeast strain GS115/bgl3A of the coding gene comprising the ?-glucosidase has high fermentation level.