99results about How to "High hydrolytic activity" patented technology

The invention discloses a higher-activity partial glyceride lipase mutant and application thereof. The mutant is an enzyme mutant prepared by carrying out site-directed mutagenesis on Malassezia globosa partial glyceride lipase, wherein the mutant site is Phe at the 278th site, and the Phe at the 278th site is mutated into Ile or Gly. The obtained mutant Phe278Ile or Phe278Gly has higher partial glyceride hydrolysis activity, and is more suitable for application in biochemical engineering industry. The partial glyceride hydrolysis activities of the modified SMG1Phe278Ile and SMG1Phe278Gly mutants are enhanced to different degrees, which are respectively 1.84 times and 1.68 times of the wild type SMG1 lipase hydrolysis activity; and the modified SMG1Phe278Ile and SMG1Phe278Gly mutants have higher partial glyceride activity, and can be used for removing partial glyceride in grease.

The invention belongs to the technical field of sulfur reclamation in the rubber ingredient industry, and in particular relates to a method for filling a sulfur production catalyst in the rubber ingredient industry, which is characterized in that the sulfur production catalyst is respectively filled into triple-stage sulfur production reactors, wherein the height of the catalyst in the triple-stage sulfur production reactors is all 800 millimeter; the upper part of a primary converter is filled with 1 cubic meter of PSR-41, and the lower part of the primary converter is filled with 2 cubic meters of PSR-31; the upper part of a secondary converter is filled with 1.1 cubic meters of the PSR-41, and the lower part of the secondary converter is filled with 2.1 cubic meters of the PSR-31; and the upper part of a tertiary converter is filled with 1.6 cubic meters of the PSR-41, and the lower part of the tertiary converter is filled with 1.6 cubic meters of the PSR-31. The method improves the sulfur conversion rate of a sulfur reclamation plant in the rubber industry.

The present invention relates to methods and enzymes for degrading hydrophobic ester pesticides and toxins. In particular, the present invention relates to the use of insect esterases, and mutants thereof, in the bioremediation of hydrophobic ester pesticides and toxins residues, such as pyrethroid residues, contaminating the environment and horticultural commodities.

The present invention relates to the use of insect esterases or lipases, or mutants thereof, as catalysts in biotransformation processes. The present invention may have application in any process involving hydrolysis, esterification, transesterification, interesterification or acylation reactions. The invention also has application in the enzymatic resolution of compounds to produce optically active compounds and has particular, but not exclusive, application to substrates having a hydrophobic moiety such as pyrethroids and fatty acid esters.

The invention discloses a sulfonated carbonaceous solid acid catalyst as well as a preparation method and application thereof to a microcrystalline cellulose hydrolysis process. The density of a sulfonic acid group on the surface of the catalyst is 0.30 to 0.80mmol / g and the density of an oxygen-containing group is 1.00 to 2.50mmol / g; the density ratio of the sulfonic acid group to the oxygen-containing group is controlled to be from (1 to 1.25) to (1 to 8.33). The catalyst has high hydrolysis efficiency and a preparation technology is simple and is suitable for large-scale production.

The invention belongs to the technical field of deep processing for peanut protein, and specifically relates to a method for producing active peptide from peanut cake and meal by immobilized enzyme. The method comprises the steps of: immobilizing two proteases, i.e. alkaline and neutral proteases, by adopting chemically-modified magnetic chitosan micro-particles so as to implement enzymatic hydrolysis, and then centrifuging, decolorizing, desalting by nano-filtration, grading by ultrafiltration and spray-drying to obtain peanut active peptide. Compared with the traditional preparation method,the method has the characteristics of low production cost, short production period, high product yield, high product purity, mild, green and energy-saving production process and the like. In additionto excellent dissolubility, the peanut functional peptide produced by the method provided by the invention has the functions of lowering blood pressure and resisting oxidation, so the active peptide has high market development value.

The invention discloses yersinia pseudotuberculosis-sourced antifungal protein and a coding gene and application thereof, and belongs to the technical field of genetic engineering. The antifungal protein is protein comprising the amino acid sequence shown as SEQ ID NO: 1, or protein obtained by substituting, deleting or inserting one or several amino acid sequences in the amino acid sequence shownas SEQ ID NO: 1 and having equivalent activity. The invention further provides the coding gene, an expression vector and engineering bacteria of the antifungal protein. The invention further providesa separation and purification method of the yersinia pseudotuberculosis-sourced antifungal protein. The protein is applied to an antifungal agent and the coding gene of the protein is applied to a transformed plant. The YPK_AFP1001 antifungal gene and the protein, related by the invention, have higher and more broad-spectrum antifungal activity.

The present invention relates to methods and enzymes for degrading hydrophobic ester pesticides and toxins. In particular, the present invention relates to the use of insect esterases, and mutants thereof, in the bioremediation of hydrophobic ester pesticides and toxins residues, such as pyrethroid residues, contaminating the environment and horticultural commodities.

The invention discloses an aspergillus oryzae lipase mutant and application thereof in disassembling (R,S)-2-(4-hydroxyphenoxy)propionate for preparing (R)-2-(4-hydroxyphenoxy)propionate. The mutant is obtained by site-saturated single or multiple mutations of the 38th site or the 230th site of the amino acid sequence in SEQ ID NO.1. By comparing the hydrolysis capability of mutant enzymes AOL-3F38N and AOL-3F38N-V230R and the non-mutated enzyme AOL-3, a user finds that the hydrolytic activity of the mutant enzymes AOL-3F38N and AOL-3F38N-V230R is 3.4 times and 4.0 times that of the non-mutated lipase, the thermal stability of the modified lipase is better after 50 DEG C, and the yield of the (R)-2-(4-hydroxyphenoxy)propionate is increased. The mutant is more suitable for industrial production.

The invention provides tertiary alcohol ester hydrolase, a gene for encoding the same, a carrier containing the encoding gene, engineering bacteria and application thereof. The amino acid sequence of the tertiary alcohol ester hydrolase is shown as SEQ ID No.2, and the amino acid sequence of the encoding gene is shown as SEQ ID No.1. The tertiary alcohol ester hydrolase is high in short-carbon chain ester hydrolytic activity; and the enzymatic activity for catalyzing hydrolysis of p-nitrophenol butyrate in a Tri-HCl buffer solution with pH of 8.5 at the temperature of 50 DEG C can reach 3,010 U / mg. The esterase is high in strong organic solvent resistance stability and activity improving characteristic; and after the esterase is incubated in strong organic solvents such as normal hexane, toluene and dimethylbenzene, of which the partition coefficient Log P is greater than 3, the enzymatic activity still can be improved by 51 percent, 44 percent and 49 percent respectively. Moreover, the esterase has tertiary alcohol ester hydrolytic activity, so that the esterase can be widely used for hydrolyzing different tertiary alcohol ester substrates. The esterase, the encoding gene, the carrier, and the recombinant bacteria can be widely applied to ester catalysis of synthesis and resolution of chiral compounds related to tertiary alcohol substrates in medicine industry, food industry, chemical industry and the like.