Abstract

Streptococcus suis, and has a low hemolytic activity against mouse red blood cells and a low murine macrophage cytotoxicity.

IPC Classes  ?

• C07K 14/39 - Peptides having more than 20 amino acidsGastrinsSomatostatinsMelanotropinsDerivatives thereof from fungi from yeasts
• C12N 1/16 - YeastsCulture media therefor
• C12N 15/81 - Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts

Abstract

The present invention relates to the field of genetic engineering, and specifically relates to a mutant glucose oxidase (GOD) having improved thermal stability and a gene and application thereof. The mutant glucose oxidase is mutated sequentially by wild-type site direction to obtain a plurality of mutants having significantly improved thermal stability and catalytic efficiency. The glucose oxidase mutant has good enzymatic properties, and can be used in livestock feed, food products, medicine, textiles, and other industries.

IPC Classes  ?

• C12N 9/04 - Oxidoreductases (1.), e.g. luciferase acting on CHOH groups as donors, e.g. glucose oxidase, lactate dehydrogenase (1.1)
• C12N 15/53 - Oxidoreductases (1)
• C12N 15/81 - Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts

Abstract

Disclosed is the use of an HIF1α protein as a biomarker in the screening of a safe liver fat-lowering feed additive. Aquatic animals can be fed with the feed additive, and the expression quantity of the HIF1α protein in the intestines before and after feeding is then detected, and if the expression quantity of the HIF1α protein in the intestines after feeding is not lower than that before feeding, the feed additive does not cause liver inflammation, liver damage, or alteration of the intestinal flora.

IPC Classes  ?

• C12N 1/20 - BacteriaCulture media therefor
• C12Q 1/68 - Measuring or testing processes involving enzymes, nucleic acids or microorganismsCompositions thereforProcesses of preparing such compositions involving nucleic acids
• C12Q 1/04 - Determining presence or kind of microorganismUse of selective media for testing antibiotics or bacteriocidesCompositions containing a chemical indicator therefor
• A61K 45/00 - Medicinal preparations containing active ingredients not provided for in groups
• A61P 1/16 - Drugs for disorders of the alimentary tract or the digestive system for liver or gallbladder disorders, e.g. hepatoprotective agents, cholagogues, litholytics
• A61P 1/00 - Drugs for disorders of the alimentary tract or the digestive system
• A61P 31/00 - Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
• A23K 10/18 - Addition of microorganisms or extracts thereof, e.g. single-cell proteins, to feeding-stuff compositions of live microorganisms
• A23K 20/163 - SugarsPolysaccharides
• A23K 20/10 - Organic substances
• A23K 50/80 - Feeding-stuffs specially adapted for particular animals for aquatic animals, e.g. fish, crustaceans or molluscs

Abstract

th site 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.

IPC Classes  ?

• C12N 9/16 - Hydrolases (3.) acting on ester bonds (3.1)
• C12N 1/21 - BacteriaCulture media therefor modified by introduction of foreign genetic material
• C12N 15/55 - Hydrolases (3)
• A23K 20/189 - Enzymes
• C12N 15/52 - Genes encoding for enzymes or proenzymes
• C12N 15/70 - Vectors or expression systems specially adapted for E. coli

Abstract

Provided is a glucoamylase TlGa15 derived from a fungus, and a gene and an application thereof. The amino acid sequence is shown in SEQ ID NO.1 or SEQ ID NO.2. The glucoamylase may be applied to feed, food, medicine and other industries.

IPC Classes  ?

• C12N 9/34 - Glucoamylase
• C12N 15/56 - Hydrolases (3) acting on glycosyl compounds (3.2), e.g. amylase, galactosidase, lysozyme
• C12N 15/81 - Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts
• C12N 1/19 - YeastsCulture media therefor modified by introduction of foreign genetic material
• C12R 1/84 - Pichia

Abstract

Provided are a recombinant expression vector applicable to rapid screening for a high-expression strain and a rapid screening method for a high-expression strain. The method comprises fused expression of exogenous red fluorescent protein (DsRed) and a localization signal peptide of a cell surface protein from Aspergillus fumigatus (AfMP1), and integration of the fused gene (DsRed-AfMP1) into the genome of Trichoderma reesei, thereby constructing a strain expressing red fluorescent protein on the surface of Trichoderma reesei. The Trichoderma reesei strain expressing red fluorescent protein on the surface are sorted by means of a flow cytometer, so as to quickly isolate genetic changes beneficial to increasing cellulase activity.

IPC Classes  ?

• C12N 15/80 - Vectors or expression systems specially adapted for eukaryotic hosts for fungi

Abstract

Aspergillus nigerAspergillus niger as a female parent, which is subjected to point mutation to obtain a glucose oxidase GOD-M5 having improved catalytic efficiency and thermal stability. The specific activity of the mutant of the present invention is increased by 66% relative to a wild type GOD. After 10 minutes of treatment at 70°C, the enzyme activity of the mutant of the present invention is increased by 13.6 times compared with the wild type. After 2 minutes of treatment at 80°C, the enzyme activity of the mutant of the present invention is increased by 29.4 times compared with the wild type.

IPC Classes  ?

• C12N 9/04 - Oxidoreductases (1.), e.g. luciferase acting on CHOH groups as donors, e.g. glucose oxidase, lactate dehydrogenase (1.1)
• C12N 15/53 - Oxidoreductases (1)
• C12N 15/81 - Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts

Abstract

A mannanase mutant having improved heat resistance, a gene thereof, and an application. A penicillium-derived GH5 family mannanase PMan5A is used as a parent, and molecular biological means are used to mutate histidine (H), phenylalanine (F), leucine (L) and alanine (A) at sites 93, 94, 356 and 389 in the parent into tyrosine (Y), tyrosine (Y), histidine (H) and proline (P). Result show that single-point mutants H93Y, L356H and A389P all have better heat resistance than wild-type PMan5A, and the heat resistance of a combination mutant shows a synergistic effect of the single-point mutations, indicating that sites 93, 94, 356 and 389 of PMan5A play an important role in the heat resistance of GH5 family mannanase.

IPC Classes  ?

• C12N 9/42 - Hydrolases (3.) acting on glycosyl compounds (3.2) acting on beta-1, 4-glucosidic bonds, e.g. cellulase
• C12N 15/81 - Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts
• C12R 1/84 - Pichia

Abstract

The present invention relates to the field of agricultural biotechnology and specifically relates to an amylase mutant having high specific activity and thermal stability, the gene of the mutant, and applications thereof. A wild-type amylase of which the amino acid sequence is as represented by SEQ ID NO. 1 undergoes an S33A/S34E/V35H point mutation and the amino acids at loci 178 and 179 are removed, thus acquiring the amylase mutant. Compared with the wild-type amylase, the amylase mutant of the present invention has the following traits: 1) enhanced amylase activity; and 2) enhanced amylase thermal stability.

IPC Classes  ?

• C12N 9/28 - Alpha-amylase from microbial source, e.g. bacterial amylase
• C12N 15/56 - Hydrolases (3) acting on glycosyl compounds (3.2), e.g. amylase, galactosidase, lysozyme
• C12N 15/75 - Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora for Bacillus

Abstract

AeromonasAeromonas veroniiAeromonas veroniiAeromonas hydrophilaAeromonas Aeromonas vaccine, and/or a hemorrhagic disease vaccine for an aquaculture animal.

IPC Classes  ?

• C12N 1/21 - BacteriaCulture media therefor modified by introduction of foreign genetic material
• A61K 39/02 - Bacterial antigens
• A61P 31/04 - Antibacterial agents
• A61P 7/04 - AntihaemorrhagicsProcoagulantsHaemostatic agentsAntifibrinolytic agents
• C12R 1/01 - Bacteria or actinomycetales

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.

IPC Classes  ?

• C12N 9/08 - Oxidoreductases (1.), e.g. luciferase acting on hydrogen peroxide as acceptor (1.11)
• C12N 15/53 - Oxidoreductases (1)
• C12N 15/70 - Vectors or expression systems specially adapted for E. coli

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 the glucose oxidase CnGODA and an application of the glucose oxidase CnGODA.

IPC Classes  ?

• C12N 9/04 - Oxidoreductases (1.), e.g. luciferase acting on CHOH groups as donors, e.g. glucose oxidase, lactate dehydrogenase (1.1)
• C12N 15/53 - Oxidoreductases (1)
• C12N 15/81 - Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts

Abstract

Phytase YeAPPA mutants having improved gastric protein resistance and acid resistance and increased catalytic efficiency. Leucine at a 162th position of a phytase having an amino acid sequence as shown in SEQ ID NO. 1 is mutated to become glycine or alanine, or glutamic acid at a 230th position is mutated to become glycine, proline or arginine. Compared to the wild type, the pepsin resistance and acid resistance of the mutants increased significantly, while the catalytic efficiencies increased by 1.6 times and 2.4 times respectively, which is favorable for the development of the resource-saving feed enzyme industry.

IPC Classes  ?

• C12N 9/16 - Hydrolases (3.) acting on ester bonds (3.1)
• C12N 15/55 - Hydrolases (3)
• A23K 20/189 - Enzymes

Abstract

A phytase YkAPPA mutant having improved pepsin resistance and increased catalytic efficiency. Leucine at position 162 of the phytase amino acid sequence as shown in SEQ ID NO. 1 is mutated to glycine or alanine, or glutamic acid at position 230 is mutated to glycine, alanine, proline, arginine, serine, threonine or aspartic acid.

IPC Classes  ?

• C12N 9/16 - Hydrolases (3.) acting on ester bonds (3.1)
• C12N 15/55 - Hydrolases (3)
• C12N 15/70 - Vectors or expression systems specially adapted for E. coli
• A23K 20/189 - Enzymes
• C12N 1/21 - BacteriaCulture media therefor modified by introduction of foreign genetic material
• C12R 1/19 - Escherichia coli

Abstract

Provided are an acidic thermophilic polygalacturonase TePG28A, and an encoding gene and an 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 prospects; can effectively degrade pectic substances such as polygalacturonic acid and pectin; and can be effectively applied to the industrial fields of feed, food, textile, etc.

IPC Classes  ?

• C12N 9/24 - Hydrolases (3.) acting on glycosyl compounds (3.2)
• C12N 15/56 - Hydrolases (3) acting on glycosyl compounds (3.2), e.g. amylase, galactosidase, lysozyme
• C12N 15/81 - Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts
• C12N 1/19 - YeastsCulture media therefor modified by introduction of foreign genetic material

Abstract

Provided are a fungus-sourced high-temperature acid β-glucosidase as well as a coding gene and an application thereof. The provided β-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 β-glucosidase has high fermentation level.

IPC Classes  ?

• C12N 9/42 - Hydrolases (3.) acting on glycosyl compounds (3.2) acting on beta-1, 4-glucosidic bonds, e.g. cellulase
• C12N 15/56 - Hydrolases (3) acting on glycosyl compounds (3.2), e.g. amylase, galactosidase, lysozyme
• C12N 15/81 - Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts

Abstract

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

IPC Classes  ?

• C12N 9/42 - Hydrolases (3.) acting on glycosyl compounds (3.2) acting on beta-1, 4-glucosidic bonds, e.g. cellulase
• C12N 15/56 - Hydrolases (3) acting on glycosyl compounds (3.2), e.g. amylase, galactosidase, lysozyme
• C12N 15/63 - Introduction of foreign genetic material using vectorsVectorsUse of hosts thereforRegulation of expression
• C12N 1/16 - YeastsCulture media therefor
• C12R 1/85 - Saccharomyces

Abstract

Provided is a method for preparing glyceryl tributyrate, comprising: using an organic base as an acid-binding agent to cause glycerin to react with butyryl chloride and obtain a mixture containing glyceryl tributyrate. The molar ratio of the three materials glycerin, butyryl chloride and organic base is 1:(3-3.3):3.3. The method further comprises extracting with water the mixture containing glyceryl tributyrate, collecting organic phase, and vaporizing under reduced pressure to remove the solvent from the organic phase to obtain glyceryl tributyrate. The molar ratio of butyryl chloride and glycerin during reaction remains 3-3.3:1, without substantial excess. Furthermore, a minor amount of butyryl chloride residuals after the reaction is completed can be hydrolyzed to butanoic acid and hydrochloric acid in a subsequent water washing process, and carried away with the residual glycerin by the water phase, achieving an objective of isolating from the target product.

IPC Classes  ?

• C07C 67/14 - Preparation of carboxylic acid esters from carboxylic acid halides
• C07C 69/30 - Esters of acyclic saturated monocarboxylic acids having the carboxyl group bound to an acyclic carbon atom or to hydrogen having three or more carbon atoms in the acid moiety esterified with trihydroxylic compounds

Abstract

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 from Escherichia coli and 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.

IPC Classes  ?

• C12N 9/16 - Hydrolases (3.) acting on ester bonds (3.1)
• C12N 15/55 - Hydrolases (3)
• C12N 15/63 - Introduction of foreign genetic material using vectorsVectorsUse of hosts thereforRegulation of expression
• C12N 1/14 - Fungi Culture media therefor
• C12N 1/21 - BacteriaCulture media therefor modified by introduction of foreign genetic material
• A23K 1/165 - with steroids, hormones, or enzymes

Abstract

Provided are a mutant of xylanase XynAS9-m with an improved thermal stability and a gene and use thereof. The mutant of xylanase XynAS9-m has an amino acid sequence with the valine at position 81 of xylanase mutated into proline, and the glycine at position 82 mutated into glutaminic acid as shown in SEQ ID No. 1. Further, the aspartic acid at position 185 of xylanase is mutated into proline, and the serine at position 186 is mutated into glutamic acid. The thermal stability of the mutant enzyme is significantly improved, showing potential application value in pulp making, biological energy sources and other industries.

IPC Classes  ?

• C12N 15/56 - Hydrolases (3) acting on glycosyl compounds (3.2), e.g. amylase, galactosidase, lysozyme
• C12N 15/63 - Introduction of foreign genetic material using vectorsVectorsUse of hosts thereforRegulation of expression
• C12N 1/21 - BacteriaCulture media therefor modified by introduction of foreign genetic material
• C12N 9/42 - Hydrolases (3.) acting on glycosyl compounds (3.2) acting on beta-1, 4-glucosidic bonds, e.g. cellulase
• C12N 1/15 - Fungi Culture media therefor modified by introduction of foreign genetic material

Abstract

Disclosed are a novel use of Chi92 protein and a bacterial strain expressing the Chi92 protein. The preservation number of Pichia pastoris provided in the present invention is CGMCC No.7634. Also disclosed are a fermentation product of the Pichia pastoris pPIC9/Chi92, and uses of the fermentation product in the preparation of chitinases, in serving as chitinases, and in the degradation of chitin substrates. Also disclosed are the uses of the Chi92 protein in the preparation of chitinases, in serving as chitinases, and in the degradation of chitin substrates.

IPC Classes  ?

• C12N 1/19 - YeastsCulture media therefor modified by introduction of foreign genetic material
• C12N 15/56 - Hydrolases (3) acting on glycosyl compounds (3.2), e.g. amylase, galactosidase, lysozyme
• C12N 9/42 - Hydrolases (3.) acting on glycosyl compounds (3.2) acting on beta-1, 4-glucosidic bonds, e.g. cellulase
• C12R 1/84 - Pichia

Abstract

The present invention discloses autolytic recombinant bacteria, a preparation method and an application thereof. The recombinant bacteria are prepared using a method comprising the following steps: introducing E7 lysis protein-encoding genes and target protein-encoding genes into starting bacteria and obtaining engineered bacteria. Said E7 lysis protein is a protein as shown in sequence 2 of the sequence table; and/or, said target protein is a quenching enzyme; specifically, said quenching enzyme can be the protein shown in sequence 5 of the sequence table. Using the method provided in the present invention to obtain recombinant bacteria having an autolytic function can reduce the recombinant bacteria wall-breaking step of the target protein preparation process, thus decreasing the production cost of the target protein.

IPC Classes  ?

• C12N 1/21 - BacteriaCulture media therefor modified by introduction of foreign genetic material
• C12N 15/63 - Introduction of foreign genetic material using vectorsVectorsUse of hosts thereforRegulation of expression
• C12P 21/02 - Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
• C12R 1/19 - Escherichia coli

Abstract

Provided is a C-terminal domain of xylanase XynA originally from a rumen and a method for improving xylanase catalytic efficiency. A new xylanase with high efficiency is provided. The optimum pH of the xylanase in the present invention is 6.0 and the optimum temperature thereof is 50 degrees centigrade. It is found in the present invention that the C-terminal domain of the xylanase can improve its ability of substrate-degrading, producing more monosaccharides so as to improve its catalytic efficiency. It is found that the function of improving degradation ability is also applied to other xylanases by fusion expression.

IPC Classes  ?

• C12N 9/42 - Hydrolases (3.) acting on glycosyl compounds (3.2) acting on beta-1, 4-glucosidic bonds, e.g. cellulase
• C12N 15/56 - Hydrolases (3) acting on glycosyl compounds (3.2), e.g. amylase, galactosidase, lysozyme
• C12N 15/11 - DNA or RNA fragmentsModified forms thereof
• C12N 15/63 - Introduction of foreign genetic material using vectorsVectorsUse of hosts thereforRegulation of expression
• C12N 1/19 - YeastsCulture media therefor modified by introduction of foreign genetic material
• C12N 1/21 - BacteriaCulture media therefor modified by introduction of foreign genetic material

Abstract

A method of preparing yeast strains (especially Pichia pastoris) for multi-copy expression of recombinant plectasin. The method comprises: optimizing the gene sequence of plectasin according to codon bias of Picha pastoris; fusing the optimized gene to the α-factor signal peptide C-terminal of the expression vector pPICZ α A to construct a single-copy expression vector containing a plectasin expression cassette composed of an initial signal component alcohol:oxygen dehydrogenase strong promoter, an α-factor signal peptide gene and a plectasin gene fused to the C-terminal thereof, and a termination signal component; using the mutually-complementing characteristics of the sticky ends of restriction endonucleases BglII and BamHI to obtain, by repeated digestion, ligation and transformation, recombinant plasmid with a tandem expression cassette containing different copies of the plectasin gene; and transforming the recombinant plasmid into Pichia pastoris. The yeast strains can achieve highly-efficient secretory expression of plectasin under methanol induction.

IPC Classes  ?

• C12N 1/19 - YeastsCulture media therefor modified by introduction of foreign genetic material
• C12N 15/69 - Increasing the copy number of the vector
• C12N 15/81 - Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts
• C12R 1/84 - Pichia
• C12R 1/865 - Saccharomyces cerevisiae
• C12R 1/78 - Hansenula

Abstract

The present invention relates to a novel phytase enzyme, a novel isolated nucleic acid molecule coding the enzyme, and a novel Yersinia intermedia having phytase activity. Particularly, the present invention relates to the phytase having (a) Theoretical molecular weight 45.5 kDa, (b) high specific activity 3960±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°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., Pichia pastoris ) 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.

IPC Classes  ?

• C12N 9/16 - Hydrolases (3.) acting on ester bonds (3.1)
• C12N 9/52 - Proteinases derived from bacteria
• C12N 15/55 - Hydrolases (3)
• C12N 15/63 - Introduction of foreign genetic material using vectorsVectorsUse of hosts thereforRegulation of expression
• C07K 14/195 - Peptides having more than 20 amino acidsGastrinsSomatostatinsMelanotropinsDerivatives thereof from bacteria
• C12P 21/00 - Preparation of peptides or proteins
• A23K 1/165 - with steroids, hormones, or enzymes
• C12R 1/01 - Bacteria or actinomycetales