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

Ternary nanometer catalyst used for hydrolyzing ammonia borane to release hydrogen and preparation method of ternary nanometer catalyst

The invention provides a ternary nanometer catalyst used for hydrolyzing ammonia borane to release hydrogen and a preparation method of the ternary nanometer catalyst. The catalyst takes a metal-organic framework material of MIL-101 as a carrier and sodium borohydride as a reducing agent, and the multiple catalyst of RuCuCo@MIL-101 is obtained by reducing precursors of ruthenium salts, copper salts and cobalt salts. The specific surface area of the multiple catalyst synthesized with the preparation method reaches up to 2868m<2>/g, the grain size is around 6.9nm, good catalytic activity is exerted by catalyzing the ammonia borane to be hydrolyzed to release the hydrogen under the room temperature, transformation frequency (TOF) is 241.2mol H2 min<1> (mol Ru)<1>, and activation energy (Ea) is 48 kJ mol<1>. The catalyst is still good in stability after circulation tests are performed for 5 times; the ternary nanometer catalyst doped with non-noble metal has the advantages of even distribution of the metal particles, large specific surface area, more in catalytic active sites and the like, and compared with a conventional noble-metal catalyst, the ternary nanometer catalyst is low in cost, simple in preparation, easy to obtain raw materials, suitable for industrial production and good in application prospect.
Owner:HUBEI UNIV

Feruloyl esterase and preparing method and application thereof

The invention provides feruloyl esterase and a preparing method and application thereof. A feruloyl esterase gene coming from a soil macro gene library have the nucleotide sequence and amino acid sequence shown in SEQ ID NO.1 and SEQ ID NO.2. The gene contains a tetrapeptide SXXK sequence motif which is rarely seen, and after the esterase gene is inserted into plasmid pET28a(+), the gene is transformed into escherichia coli BL21(DE3) to achieve heterogeneous expression. The molecular weight of purified recombinase (DLFae4) is 38.3 kDa. Besides, it is put forward for the first time that novel feruloyl esterase can hydrolyze penbritin, penicillin, cefazolin and other lactam antibiotics. As is shown by site-directed mutagenesis experiments, a catalysis triplet of DLFae4 is composed of serine(S11), histidine (H74) and aspartic acid (D302), and the mutation of any of serine (S11), histidine (H74) and aspartic acid (D302) can cause loss of the catalysis capability of DLFae4. DLFae4 has a high hydrolytic activity on methyl ferulate and has good heat stability. In the presence of cellulase, DLFae4 can obviously increase the amount of ferulic acid released from destarched wheat bran. Due to peculiar activities and enzymatic characteristics of novel feruloyl esterase, novel feruloyl esterase can be applied to feed, paper making, food, pharmacy and other fields.
Owner:NANJING AGRICULTURAL UNIVERSITY

Tertiary alcohol ester hydrolase, encoding gene, carrier, engineering bacteria and application thereof

ActiveCN102796715AIncrease vitalityHigh resistance to organic solvents and stabilityBacteriaHydrolasesChemical industryEster hydrolase
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.
Owner:HANGZHOU NORMAL UNIVERSITY

Nematophagous fungi infectious extracellular serine proteinase crystal morphology

The invention relates to an extracellular serine protease crystal structure with nematophagous fungi infectivity and belongs to the fields of molecular biology and applied microbiology. The invention implements liquid cultivation with Lecanicillium psalliotae YMF1.00112 and Paecilomyces lilacinus M-14, fractional precipitation of ammonium sulphate with a fermented liquid, and dissolution of protease-containing active component with buffer solution, and then obtains raw enzyme solution. Cation exchange chromatography and molecular sieve purification of the raw enzyme solution are implemented. After purified enzyme is obtained, concentration processing is implemented so as to obtain an enzyme solution with higher concentration. Hanging drop vapor diffused crystallization of the enzyme solution with higher concentration is implemented. The crystallization conditions are filtered with a reagent kit. Enough diffraction pictures of obtained crystal are collected through diffraction on an X-ray machine. The diffraction pictures are processed with HKL2000, protein structure is analyzed and optimized with software O, ccp4 and the like. The invention discloses the extracellular serine protease crystal structure for the first time and provides foundation for improving the hydrolysis activity of protease and the infectivity of nematophagous fungi.
Owner:YUNNAN UNIV

Filling method for sulfur recycled catalyst with high content of CO2 in raw material gas to be treated

The invention relates to a filling method for sulfur recycled catalyst with a high content of CO2 in a raw material gas to be treated, which belongs to the method of preparing sulfur from a sulfur compound in a gaseous state of sulfides in the gaseous state. By the adoption of a two-stage sulfur preparation and conversion process, multi-functional sulfur recycled catalyst with high hydrolysis activity of organic sulfur is filled at the height from one thirds to a half in the upper part of the first-stage converter, and alumina base sulfur recycled catalyst with a large ratio surface is filled at the height from two thirds to a half in the lower part of the first-stage converter; the second-stage converter is totally filled with alumina base sulfur recycled catalyst with the large ratio surface. According to the filling method for sulfur recycled catalyst with the high content of CO2 in the raw material gas to be treated, the hydrolysis activity of sulfur is increased, and the Claus activity can be maintained high, the gas volume of CO2 in the raw material gas to be treated is as high as 50 percent, the total sulfur conversion rate of the sulfur recycle device can reach above 96 percent, and the service life of the catalyst can reach more than six years. The filling method provided by the invention is suitable for the sulfur recycling devices of facilities in petroleum refining and production, coal chemical industry and natural gas purifying.
Owner:CHINA PETROLEUM & CHEM CORP

Tertiary alcohol ester hydrolase, encoding gene, carrier, engineering bacteria and application thereof

ActiveCN102796715BIncrease vitalityHigh resistance to organic solvents and stabilityBacteriaHydrolasesChemical industryEster hydrolase
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.
Owner:HANGZHOU NORMAL UNIVERSITY
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