Other

Chinese Academy of Agricultural Sciences

Feed Research Institute Chinese Academy of Agricut

Institute of Animal Science of Chinese Academy

Feed Research Institute, Chinese Academy of Agricu

Huiying Luo

Jie Zhang

Bin Yao

Huoqing Huang

Yaru Wang

Yingguo Bai

Xiaoyun Su

Kun Meng

Yuan Wang

Tao Tu

Peilong Yang

Rui Ma

Pengjun Shi

Xia Shi

Weina Liu

Canfang Niu

Yangyang Li

Hong Yang

Fei Gao

Wei Xia

Yuan Gu

Jin Qiu

Yujie Guo

Yongkai Du

Dali Yu

Jianzhong Ge

Yeqing Li

Chao Shao

Heng Zhao

Tiezheng Yuan

Xiuyun Shi

Huang Qin

Jianshuang Ma

Xiao Jiang

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 andcell surface protein localization signal are fused and expressed, and the fusion gene (DsRed-AfMP1) is integrated into the genome of, so as to construct a strain displaying red fuorescent protein on the surface of. By sortingstrains with red fluorescent protein on the surface by flow cytometry, genes beneficial to the improvement of cellulase activity can be quickly isolated.

Recombinant expression vector applicable to rapid screening for recombinant strain and application

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.

Glucoamylase TLGA15 and gene and application thereof

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.

Manganese peroxidase, gene thereof, and use thereof in detoxification of mycotoxin

The present invention takes the glucose oxidase GOD fromas 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&#xb0; 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&#xb0; C. for 2 min.

Glucose oxidase GOD mutant and gene and application thereof

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.

Mannanase PMAN5A mutant having improved heat resistance, gene thereof, and application

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.

Amylase mutant having high specific activity and thermal stability, gene of mutant, and applications thereof

The present invention relates to the field of genetic engineering, particularly to phytase variant YeAPPA having improved pepsin resistance and acid resistance, and increased catalytic efficiency, by substituting Leucine at the 162site of the sequence set forth in SEQ ID NO.1 with glycine or proline or substituting glutamic acid at the 230site of the sequence set forth in SEQ ID NO.1 with glycine, proline or arginine, in the benefit of the development of economical feed enzyme industry.

Phytase variants YeAPPA having improved gastric protein resistance and acid resistance, and increased catalytic efficiency

The present invention relates to the field of genetic engineering, particularly to phytase variants YkAPPA having amino acid sequence substituting Leucine at the 162site of the sequence set forth in SEQ ID NO.1 with glycine or proline, or having amino acid sequence substituting glutamic acid at the 230site of the sequence set forth in SEQ ID NO.1 with glycine, alanine, serine, threonine, aspartic acid, proline, or arginine, and having improved pepsin resistance and increased catalytic efficiency of 2.1 times of that of the wild phytase, in the benefit of the development of economical feed enzyme industry.

Phytase variants YkAPPA having improved pepsin resistance and increased catalytic efficiency

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.

Acidic thermophilic polygalacturonase TEPG28A, and encoding gene and application thereof

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.

Glucose oxidase CnGODA and gene and application thereof

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&#xb0; 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&#xb0; 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.

High-temperature neutral cellulase as well as coding gene and application thereof

Provided are a fungus-sourced high-temperature acid &#x3b2;-glucosidase as well as a coding gene, and an application thereof. The provide &#x3b2;-glucosidase has the optimal pH value of 4.5 and the optimal temperature of 75&#xb0; C., and maintains over 90% enzyme activity in the optimal condition after being processed at 60&#xb0; C. for 1 h. The re-engineering yeast strain GS115/bgl3A of the coding gene comprising the &#x3b2;-glucosidase has high fermentation level.

Fungus-sourced high-temperature acid B-glucosidase as well as coding gene and application thereof

The present invention relates to the field of genetic engineering, in particular, the present invention relates to a method for producing a phytase variant with an improved thermal stability, and a phytase variant and the use thereof. The phytase variant contains at least one proline modification, compared to the phytase fromand other mutants thereof. The phytase variants with the modification have preferably improved properties, such as the thermal stability, optimal reaction temperature, pH property, specific activity, protease resistance and performance in animal feeds.

Method for producing a phytase variant with improved thermal stability, and a phytase variant and the use thereof

The present invention relates to a novel phytase enzyme, a novel isolated nucleic acid molecule coding the enzyme, and a novelhaving phytase activity. Particularly, the present invention relates to the phytase having (a) Theoretical molecular weight 45.5 kDa, (b) high specific activity 3960&#xb1;248 U/mg, (c) high stability at high temperature and wide pH, (d) optimal pH of 4.0-5.0, (e) optimal temperature of 50-60&#xb0; C., (f) high resistance to pepsin and trypsin. The phytase is very suitable to be used in feed of monogastrics as feed additive. The present invention also relates to a recombinant vector comprising said nucleic acid molecule, a recombinant host cell (e.g.,) harboring said recombinant vector, and a method for producing phytase using the recombinant host cell. The present invention further provides a feed additive comprising said phytase and/or host cells expressing a phytase as effective ingredient. In addition, the present invention provides a novel method for isolating phytase from a target organism.

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Beijing, China

Huiying Luo