970 results about "Catalytic efficiency" patented technology

The invention discloses a high-performance carbonyl reductase mutant and application thereof in synthesis of a series of chiral alcohols. The high-performance carbonyl reductase mutant is obtained by performing the following mutations on an amino acid sequence as shown in SEQ ID NO.2: the 69th alanine mutates into any one of lysine, leucine, aspartic acid or asparagine, and the 69th alanine mutates into any one of lysine, leucine, aspartic acid or asparagine; and / or the 100th glycine is mutated into any one of glutamic acid, serine, lysine or asparagine. Compared with a wild type enzyme, the thermal stability and the catalytic activity of the obtained mutant are remarkably improved, particularly, single point mutants Mut-A69N, Mut-G100E and Mut-G100N and a combined mutant Mut-A69N-G100N show excellent relative enzyme activity, thermal stability and substrate tolerance. The mutant has high catalytic activity and stability to various chiral alcohols, and the contradiction that the traditional carbonyl reductase is easy to inactivate at high temperature and the catalytic efficiency is difficult to achieve at the same time is solved. The invention provides an efficient and stable enzyme catalysis tool for green biological preparation of chiral drug intermediates.

The invention discloses a high-efficiency lysine decarboxylase mutant and an application of the high-efficiency lysine decarboxylase mutant in synthesis of pentamethylene diamine. A series of mutants including a single mutant (such as N218G, T222V, C244P and the like), a double mutant and a three mutant are obtained by carrying out multi-site mutation on wild type lysine decarboxylase (SEQ ID NO.2) from Klebsiella grimontii. The catalytic efficiency of the mutant is remarkably improved, and the activity of the mutant is improved by 5.0-10.2 times compared with that of a wild type enzyme. According to the method disclosed by the invention, the substrate conversion rate of 99% or above can be realized within 2 hours through an optimized process of constructing an expression vector and a genetically engineered bacterium, inducing expression of lysine decarboxylase and synthesizing 1, 5-pentanediamine by utilizing a whole-cell catalysis technology. Compared with a traditional chemical method and a natural enzyme method, the method disclosed by the invention has the advantages of simplified process, high catalytic efficiency, low production cost and the like, and is suitable for producing bio-based 1, 5-pentamethylene diamine and nylon 56 salt.

The invention discloses a high-stability hydroxysteroid dehydrogenase mutant, a co-immobilized enzyme construction method and application. According to the invention, a site-directed mutant library is constructed based on computer-aided design, and mutants with significantly improved thermal stability and greatly improved catalytic efficiency compared with wild type mutants are obtained through screening; meanwhile, a co-immobilized enzyme construction method based on electrostatic adsorption and chemical crosslinking is established, the hydroxysteroid dehydrogenase mutant and lactic dehydrogenase are co-immobilized, the co-immobilized enzyme can still keep high activity under high substrate concentration, and the conversion rate is still maintained to be 90% or above after 30 batches of co-immobilized enzyme are repeatedly used. And an important foundation is laid for industrial application of the hydroxysteroid dehydrogenase.

The invention belongs to the technical field of microbial genetic engineering, and particularly relates to an alpha-2, 3-sialyltransferase mutant and application thereof. The a-2, 3-sialyltransferase mutants V175N, P198A, G173D, D174Q, F196K and A315H are obtained by performing site-specific mutagenesis on six amino acids in an a-2, 3-sialyltransferase amino acid sequence coded by a gene derived from Campylobacter jejuni (OH4384), the yield of 3 '-sialyllactose is remarkably increased by single-point mutagenesis of the V175N, the yield of 3'-sialyllactose is remarkably increased by single-point mutagenesis of the V175N, the yield of 3 '-sialyllactose is remarkably increased by single-point mutagenesis of the P198A, the G173D, the D174Q, the F196K and the A315H, the optimal recombinant microbial strain 3 '-SL-09 (V175N / P198A / D174Q) is obtained through combination of multiple mutation sites, the yield can reach 5.91 g / L, the bottleneck problem of low catalytic efficiency of sialyltransferase is effectively solved, and an enzyme element with excellent performance is provided for high-efficiency and low-cost biological manufacturing of 3'-SL.

The invention discloses preparation of a high-performance carbon matrix embedded iron-based catalyst based on a metal organic framework precursor and application of the high-performance carbon matrix embedded iron-based catalyst in reverse water-gas shift reaction. In the preparation process, commercially available 1, 3, 5-trimesic acid iron (the chemical formula is C9H3FeO6, abbreviated as Fe-BTC) is selected as a raw material, pyrolysis treatment is carried out in an argon atmosphere, then air passivation is carried out, and finally the high-performance carbon matrix embedded iron-based catalyst based on the metal organic framework precursor is successfully prepared. The MOF-600 has excellent performance in many catalysts, the carbon dioxide production rate reaches 24.0 mmol CO.gcat <-1 >. S <-1 > at the temperature of 400 DEG C in a reverse water gas shift reaction, the performance is remarkably superior to that of an existing non-noble metal catalyst, and extremely high catalytic efficiency and application potential are shown.

The invention discloses an endoglucanase truncated mutant and an application of the endoglucanase truncated mutant. According to the invention, based on endoglucanase BsEGL from bacillus subtilis DLG, a truncated mutant is constructed by deleting a carbohydrate binding domain (CBM) of the endoglucanase BsEGL, and the truncated mutant is named as BsEGL [delta] CBM. Compared with BsEGL, the truncated mutant BsEGL delta CBM has the advantages that the thermal stability, the pH stability, the organic solvent tolerance and the like are remarkably improved, and the activity of degrading phosphoric acid expanded cellulose and corncob xylan is obtained. In addition, the enzymatic activity of the truncated mutant BsEGL delta CBM is remarkably improved by 6.41%, and the catalytic efficiency is remarkably improved. Due to the characteristics, the mutant can be suitable for industrial processes such as feed processing, papermaking, biological energy sources, spinning and food brewing, and is particularly suitable for enzyme catalytic reaction under extreme environments such as high temperature and low pH. The invention provides an enzyme preparation tool with excellent performance for efficient degradation of cellulose biomass, and has important application value.

The invention relates to the field of nano-enzymes, in particular to a nano-enzyme, a preparation method and a method for detecting glucose by using the nano-enzyme. The nano-enzyme comprises a carrier and platinum nano-particles coated on the surface of the carrier, and the carrier is oxidized nano-diamond particles with the particle size of 20-30 nm. The core structure of the nano-enzyme, namely a composite system of the carrier and the platinum nano-particles, is defined, the platinum nano-particles serve as a metal nano-material with excellent catalytic performance and are a core component for simulating peroxidase activity, the size of the oxidized nano-diamond carrier is controlled to be 20-30 nm, the dispersity of the material is guaranteed, and the catalytic activity of peroxidase is improved. And the catalytic efficiency of the composite system can be further improved through a size effect. According to the structural design, the problems of insufficient catalytic activity and poor stability of a single nano material are solved through the synergistic effect of the carrier and the load component, and a material foundation is laid for subsequent efficient glucose detection.

The invention discloses NnLuz and NnH3H protein mutants and an application of the NnLuz and NnH3H protein mutants in enhancing the bioluminescence intensity of fungi or plants. According to the method disclosed by the invention, core enzymes NnLuz and NnH3H in a fungus bioluminescence pathway are optimized through rational design, and the catalytic efficiency and the luminous intensity of a bioluminescence system are remarkably improved. Experiments prove that 1) the luminous intensity of the NnLuz [delta] N19v2 (I103T / L167K double mutant) in yeast and plants is remarkably superior to that of a reported NnLuzv4 mutant and is 3-4 times that of the reported NnLuzv4 mutant, 2) the catalytic efficiency of the NnH3Hv3 (K307T mutant) is improved by more than 2 times, the luminous stability is remarkably enhanced, and 3) when the NnLuz [delta] N19v2 and the NnH3Hv3 are cooperatively expressed, the luminous intensity of the system reaches the optimal level, and the self-luminous plant with remarkably enhanced luminescence is created.

The invention provides an oxygen vacancy defect carbon nitride anchored iron atom cluster catalyst and a preparation method and application thereof, and belongs to the technical field of catalysts. Iron atoms are anchored in a carbon nitride (Ov-C3N4) structure containing oxygen vacancy defects in a cluster form, and Fe-Ov-C defect bonds are formed between the oxygen vacancy defects in C3N4 and iron atom clusters to stabilize the iron atom clusters, so that the problem of thermodynamic instability of the catalyst is solved while higher atom utilization efficiency is obtained; the Fe-Ov-C defect bond atoms can reasonably regulate and control the electronic structure of the center of an iron cluster d band, so that the catalytic activity and the cycling stability are greatly enhanced; besides, iron atom clusters and persulfate act to cause O-O bond breakage, non-free radical singlet oxygen is formed, and the problem that the catalytic efficiency is sharply reduced due to free radical annihilation in a complex water environment can be effectively solved.

The invention relates to the technical field of biological catalysis, and discloses an L204A mutant enzyme for preparing rebaudioside I. The enzyme is obtained by the following mutations generated by UGT76G1: L204A: leucine of the 204 amino acid sequence of UGT76G1 mutates into alanine; the high-efficiency in-vitro enzymatic preparation of the rebaudioside I (RI) is realized for the first time, the catalytic efficiency of the rebaudioside I (RI) is improved by more than 7 times (from about 7% to more than or equal to 50%) compared with that of an original enzyme, the high-efficiency performance can be stably maintained under different scales of 10mL to 5L, a solid foundation is laid for industrial application of the RI, and the preparation method is simple, controllable in process condition and suitable for popularization and application.

The invention relates to the technical field of enzyme engineering, in particular to an acylase mutant and a biosynthesis method of (R)-2-aminobutanol.The acylase mutant comprises at least one of mutation of the following sites relative to wild type acylase with the amino acid sequence being SEQ ID NO: 1: T106, A625 and S413. The acylase mutant disclosed by the invention is used for synthesizing (R)-2-aminobutanol through biological catalysis, and the reaction route is as follows: the catalytic efficiency of a product is remarkably improved by the mutant, and the ee value of a chiral product is improved; according to the synthesis method, the problem of chiral resolution in the prior art is solved, the production cost is reduced, and pollution is reduced.

The invention discloses a high-stability carbonyl reductase mutant and application of the high-stability carbonyl reductase mutant in chiral alcohol synthesis. An amino acid sequence as shown in SEQ ID NO.2 is mutated as follows: 20th leucine is replaced by any one of lysine, threonine, aspartic acid or isoleucine, and / or 55th leucine is replaced by any one of methionine, serine, lysine or isoleucine, and / or 55th leucine is replaced by any one of methionine, serine, lysine or isoleucine. Compared with a wild type enzyme, the stability of the obtained mutant is remarkably improved, particularly, single-point mutants Mut-L20I and Mut-L55I and a combined mutant Mut-L20I-L55I show excellent relative enzyme activity, thermal stability and substrate tolerance. The mutant has high catalytic activity and stability to various chiral alcohols, has the advantages of high catalytic efficiency, high thermal stability, strong substrate tolerance, easiness in fermentation production and the like, and is suitable for industrial application of enzymatic synthesis of chiral alcohols.

The invention discloses a preparation method of a catalytic membrane for organic wastewater treatment, which comprises the following steps: dissolving polyvinylidene fluoride (PVDF), a pore-forming agent and plant polyphenol in an organic solvent, and stirring to obtain a membrane casting solution, wherein the PVDF accounts for 12-20%, the pore-forming agent accounts for 1-8%, and the plant polyphenol accounts for 1-6%; standing and defoaming the membrane casting solution, blade-coating the membrane casting solution on a support body to form a membrane, and performing phase inversion in a water bath to obtain the plant polyphenol modified PVDF membrane; and immersing the membrane in a 3-10 mmol / L metal chloride aqueous solution, and reacting at 40-80 DEG C for 6-48 hours, so that metal ions and polyphenol are coordinated and crosslinked, and a metal-polyphenol network layer is formed on the surface of the membrane and the inner walls of membrane pores, thereby obtaining the catalytic membrane. The catalytic membrane can activate peroxymonosulfate (PMS) and synergistically degrade organic pollutants in water under a differential pressure filtration working condition, active sites are anchored stably, metal precipitation is reduced, and flux and catalytic efficiency are both considered.

The invention discloses a method for intensively leaching chromium from vanadium extraction waste slag, and belongs to the field of metallurgical chemical industry. According to the method, diboron trioxide serves as a catalyst, vanadium extraction waste slag, sodium carbonate and sodium hydroxide serve as raw materials, the raw materials and the catalyst are mixed according to a set proportion, and leaching is conducted after roasting is conducted in a microwave muffle furnace. According to the method provided by the invention, the reaction can be promoted to be efficiently carried out at medium and low temperatures, the extraction rate of chromium can reach 95% or above, and the synergistic effect of'low addition amount-high catalytic efficiency 'can be realized under the condition that a small amount of catalyst is added.

The invention relates to the field of drug-resistant bacterium infection, and discloses a g-C3N4 / Bi2Se3 nano heterojunction and a preparation method thereof.The preparation method comprises the steps that firstly, melamine powder is heated and calcined at the constant temperature, after a tubular furnace is naturally cooled, spark plasma sintering is conducted, nitrogen vacancies are introduced at the same time, and a blocky high-defect g-C3N4 material is obtained; grinding into powder, adding deionized water for ultrasonic treatment to obtain a first suspension, performing centrifugal treatment, freeze-drying the supernatant, and adding into an ethylene glycol solvent to obtain a second suspension; eG, polyvinylpyrrolidone, Bi (NO3) 3.5 H2O and Na2SeO3 are mixed and stirred, and the second turbid liquid is added; the preparation method comprises the following steps: adding Bi2Se3 into a reaction kettle, heating while stirring, adding a hydroxylamine EG solution, cooling to room temperature after reaction, centrifuging, washing, and carrying out vacuum drying on a precipitate to obtain a g-C3N4 / Bi2Se3 nano heterojunction; the problems that in the prior art, the catalytic efficiency is low, a collaborative mechanism does not achieve structure-function integrated design, the performance of a key functional material is limited, and the structural stability and biological suitability of the material are insufficient are solved.

The invention discloses a recombinant escherichia coli engineering strain for producing levodopa and application, and belongs to the technical field of genetic engineering and bioengineering. Escherichia coli WSH-Z06 is used as a starting strain, a levodopa synthesis route is constructed, and supply of cofactors is enhanced by introducing glucose dehydrogenase BmgdH; and the catalytic efficiency of the HpaB is greatly improved by modifying the entrance of the HpaB substrate tunnel. In addition, by optimizing the fermentation pH and induction time, the accumulation amount of the levodopa in the fermentation liquor reaches 60.7 g / L, the production intensity reaches 1.26 g / L / h, a foundation is laid for industrial production of the levodopa, and potential value and significance are achieved for development of synthetic biology.

The invention relates to algin lyase FsAly7Z with high activity and high thermal stability, which is mainly used for producing brown algae trisaccharide, and an engineering bacterium and application of the algin lyase FsAly7Z. The invention provides an alginate lyase FsAly7Z derived from marine uncultured microorganisms and a preparation method of the alginate lyase FsAly7Z. The FsAly7Z has extremely high thermal stability, and compared with the enzyme activity loss of more than 50% after most enzymes are treated at 40 DEG C for 60 min, the FsAly7Z shows remarkably excellent thermal stability under the same condition, and the half-life period of the FsAly7Z exceeds 24 h; the FsAly7Z can be used for efficiently degrading sodium alginate and a polyG section which is difficult to degrade, and meanwhile, the FsAly7Z also shows the catalytic efficiency superior to that of most similar enzymes; and the content of brown algae trisaccharide in the enzymolysis product is high, so that the subsequent separation and purification process can be simplified, and the production cost can be reduced. In a word, the FsAly7Z is extremely high in thermal stability and excellent in catalytic efficiency, has both economical efficiency and conversion efficiency, can efficiently produce alginate oligosaccharide, is used for analyzing the structure and function association of alginate lyase, and has wide market prospects in the fields of medicine, food industry and the like.

The invention discloses a MoO3 / TiO2 heterojunction material with a photocatalytic memory effect and application of the MoO3 / TiO2 heterojunction material in degradation of quinolone antibiotics, and belongs to the technical field of inorganic non-metallic material preparation, solar energy utilization and environmental protection. A molybdenum source precursor solution and a titanium source precursor solution are adopted to react, polyvinylpyrrolidone is used for modifying the surface of the material, the MoO3 / TiO2 heterojunction material is obtained, and the material can generate photochromic and photocatalytic memory effects under the pre-illumination effect. The memory effect provides continuous driving force for the catalytic reaction, and the activity of the material in the dark-state catalytic process is remarkably enhanced. The MoO3 / TiO2 heterojunction material disclosed by the invention shows excellent catalytic degradation performance in practical application, and particularly shows extremely high catalytic efficiency in the aspect of water pollution control.

The invention discloses a neutral phytase mutant as well as a gene and application thereof, and belongs to the technical field of enzyme engineering. The invention aims to solve the technical problems that the existing neutral phytase is poor in thermal stability, poor in acidic environment stability, narrow in pH application range, low in low-temperature catalytic efficiency and the like. According to the technical scheme, the phytase preparation PHY06 with high stability and the gene and application of the phytase preparation PHY06 are provided. The method comprises the following steps: carrying out T329G, D333V, T353F and A364F mutation on a PHY03 sequence of which the amino acid sequence is shown as SEQ ID NO.1, so as to obtain a mutant PHY06;

The invention relates to the technical field of biological catalysis, and discloses an M88F mutant enzyme for preparing rebaudioside I. The enzyme is obtained by the following mutations generated by UGT76G1: M88F: methionine of the 88th amino acid sequence of UGT76G1 is mutated into phenylalanine; and the substrate rebaudioside A (RA) can be efficiently and directionally converted into rebaudioside I (RI) with higher value. In an optimized reaction system, the conversion rate stably reaches 40%, and the catalytic efficiency is improved by more than 5-8 times compared with the common reference enzyme. The enzyme preparation has the characteristics of high catalytic activity, mild reaction conditions, simplicity and convenience in operation and the like, shows good stability and reproducibility in laboratory research and large-scale production, and has a wide industrial application prospect.

The invention belongs to the technical field of electrocatalytic nitrate reduction catalysts, and particularly relates to a graded porous hollow carbon fiber catalyst with synergistic monatomic iron and ferric oxide clusters as well as a preparation method and application of the graded porous hollow carbon fiber catalyst. The preparation method specifically comprises the following steps: stirring polyacrylonitrile and polymethyl methacrylate in an organic solvent to obtain a spinning precursor solution; the preparation method comprises the following steps: taking ferrous sulfate heptahydrate and 1, 10-phenanthroline as ligands, and stirring in an organic solvent to obtain a metal organic ligand; the preparation method comprises the following steps: stirring a spinning precursor solution and a metal organic ligand, obtaining a metal precursor-loaded composite fiber through an electrostatic spinning technology, and then carrying out pre-oxidation and high-temperature pyrolysis to obtain the composite fiber. The prepared carbon fiber has good conductivity and a unique hollow hierarchical porous structure, transmission of reactants is greatly promoted while more active sites are exposed, the carbon fiber serves as a monatomic synergistic cluster catalyst carrier, rapid transmission of electrons is facilitated, and the electro-catalysis efficiency is effectively improved.

The invention discloses an indoor intelligent formaldehyde detection and purification device and a use method thereof. The device comprises a movable shell, a self-adaptive intelligent control system, a pretreatment unit, an efficient adsorption unit and a core catalysis unit. The pre-treatment unit is used for filtering and dehumidifying, the efficient adsorption unit is used for adsorbing formaldehyde and desorbing to realize regeneration of a composite adsorbent layer, and the core catalysis unit is used for catalytically decomposing formaldehyde and desorbed formaldehyde; and the self-adaptive intelligent control system is used for acquiring outdoor air data, dynamically tracking formaldehyde pollution and regulating and controlling purification. Through three stages of units, in combination with a multi-stage cooperative processing and intelligent feedback control technology, formaldehyde is efficiently and directionally removed by virtue of a three-stage linkage mechanism of pre-adsorption enrichment, gradient desorption regeneration and catalytic deep decomposition, the selectivity is good, safety is realized, no extra volatile organic compound is released, and the catalytic efficiency is high; adsorbent regeneration improves stability and reduces cost.

The invention provides a recombinant O-succinyl-L-homoserine mercaptotransferase mutant, a coding gene thereof, a recombinant vector containing the coding gene of the mutant, a recombinant genetically engineered bacterium obtained by converting the recombinant vector, and application of the recombinant O-succinyl-L-homoserine mercaptotransferase mutant in preparation of L-methionine. The novel recombinant O-succinyl-L-homoserine mercaptotransferase mutant with high activity and high selectivity is used as a catalyst to be applied to catalysis of O-succinyl-L-homoserine for synthesis and preparation of L-methionine, a catalytic reaction system is optimized, the feed ratio and reaction conditions in the reaction are finely regulated and controlled, and the yield of L-methionine is increased. The recombinant O-succinyl-L-homoserine mercaptotransferase mutant has high enzyme activity under the optimal reaction condition, the catalytic efficiency is further improved, the purposes of reducing cost and improving efficiency are achieved, and the method has important significance in promoting industrial application of biological catalysis preparation of L-methionine.

The application provides a preparation method and application of a molybdenum carbide loaded jute derived porous carbon material, and belongs to the technical field of electrochemical catalysis. The preparation method comprises the following steps: pretreating jute fibers to obtain jute powder; placing the jute powder in a molybdenum compound containing solution to obtain a mixture, the jute powder in the mixture adsorbing the molybdenum compound, and the mass ratio of the jute powder to the molybdenum compound in the molybdenum compound containing solution being any value in 1:(2.5-6.25); and carbonizing the jute powder adsorbing the molybdenum compound at 800-900 DEG C to obtain the molybdenum carbide loaded jute derived porous carbon material. The jute fiber derived porous carbon is used as a carrier, and the precursor is fully adsorbed and combined in the molybdenum compound containing solution. By adjusting the mass ratio and the carbonization temperature, the highly dispersed and stably loaded molybdenum carbide is realized, the structural stability and catalytic activity of the molybdenum carbide based catalyst are improved, and the catalytic efficiency of the hydrogen evolution reaction is further improved.

The invention belongs to the technical field of bioengineering, and particularly relates to a phosphorylcholine cytidyltransferase mutant and application thereof. On the basis of phosphorylcholine cytidyltransferase MsCCT001, any one or more of N194D, K91E, G98S, S148A and C156V are mutated respectively, a series of phosphorylcholine cytidyltransferase mutants are obtained through screening, and the obtained mutants have the advantages that in the reaction of catalyzing phosphorylcholine and cytidine triphosphate to generate citicoline, the yield of the obtained mutants is increased, and the yield of the obtained mutants is increased. The catalytic efficiency of the compound is 1.90-2.41 times that of initial phosphorylcholine cytidyltransferase, and a biological enzyme preparation with higher catalytic capacity is provided for preparing citicoline by a biological conversion method.

The invention belongs to the field of biomedical materials, and discloses a preparation method and application of a mesoporous polydopamine nano preparation loaded with ultra-small nano enzyme. The nano preparation takes mesoporous polydopamine nanoparticles as a carrier skeleton and is combined with ultra-small nano enzyme through an in-situ reaction: the mesoporous polydopamine nanoparticles can efficiently carry drugs and accurately deliver the drugs to inflammatory tissues such as psoriasis, gout, colitis and the like by virtue of a modified targeting ligand by virtue of high specific surface area, biocompatibility and modifiability; the ultra-small nano enzyme has catalytic activity of catalase and the like, and can remove active oxygen and relieve oxidative stress. The two components are combined to achieve a synergistic effect, so that the catalytic efficiency of the enzyme is improved by virtue of the characteristics of the carrier, the high activity of the enzyme under different conditions is maintained by virtue of the stability of the carrier, and the platform can synchronously realize targeted delivery, enzymatic treatment and drug controlled release, and has a wide application prospect in the fields of inflammatory disease intervention and wound repair. And an efficient, accurate and low-toxicity universal treatment strategy is provided for chronic inflammatory diseases.

The invention discloses an electric methane preparation catalyst compounded by Ni nanoclusters and ZrO2 with lattice embedded with Ru single atoms as well as a preparation method and application of the electric methane preparation catalyst. The electric methane preparation catalyst comprises a NiNCRuSA / ZrO2 bimetallic active site catalyst compounded by the Ni nanoclusters and the ZrO2 with the lattice embedded with the Ru single atoms. The electric methane preparation catalyst comprises a NiNCRuSA / ZrO2 bimetallic active site catalyst, the NiNCRuSA / ZrO2 bimetallic active site catalyst is of a ZrO2 composite structure formed by embedding Ru monatomic into Ni nanoclusters and crystal lattices, the Ni nanoclusters and the Ru monatomic are adjacently distributed on a ZrO carrier to form a synergistic catalysis structure, rich and efficient active sites are provided for catalytic reaction, and reactant adsorption and conversion are facilitated; in the subsequent CO2 methanation reaction, the Ni element quickly dissociates H2 and provides sufficient H *, Ru replaces ZrO2 to serve as an active site for CO2 adsorption and conversion, conversion of an intermediate of CO2 can be accelerated, the reaction activity is greatly enhanced through cooperation of the Ni element and the Ru, the reaction energy barrier is reduced, and the overall catalytic efficiency is improved.

The invention discloses a cobalt-based catalytic material for efficiently activating persulfate to degrade antibiotics and a preparation method of the cobalt-based catalytic material. The catalytic material is prepared by taking an H-Beta zeolite molecular sieve as a carrier, loading cobalt ions on the molecular sieve through an impregnation method and then carrying out high-temperature roasting treatment. The preparation method comprises the following steps: preparing a cobalt acetate tetrahydrate solution, adding an H-Beta zeolite molecular sieve into the solution to carry out ion exchange, and then carrying out drying and high-temperature roasting. The prepared catalytic material has highly dispersed cobalt active sites and excellent structural stability and catalytic activity. Compared with the prior art, the catalyst provided by the invention has the advantages of simple preparation process, lower cost, high catalytic efficiency, good stability, low cobalt ion dissolution rate, easiness in recovery and reuse and the like, and has a good practical application prospect.

The invention belongs to the technical field of microbial genetic engineering, and particularly relates to an alpha-2, 6-sialyltransferase mutant and application thereof. The a-2, 6-sialyltransferase mutants M133L, E140D, D228H, N289D and G322Q are obtained by carrying out site-specific mutagenesis on five amino acids in an a-2, 6-sialyltransferase amino acid sequence coded by a gene derived from Photobacterium sp.JT-ISH-224, and compared with wild type alpha-2, 6-sialyltransferase, the yield of the single-point mutant 6 '-SL of the E140D and the yield of the single-point mutant 6'-SL of the G322Q are increased by 87.80% and 78.01% respectively. The yield of the optimal recombinant microbial strain 6 '-SL-7 (E140D / G322Q) obtained by mutation site combination can reach 1.471 g / L, the bottleneck problem of low catalytic efficiency of sialyltransferase is effectively solved, and an enzyme element with excellent performance is provided for high-efficiency and low-cost biological manufacturing of 6'-SL.

The invention relates to the technical field of biology, in particular to a carbonyl reductase mutant, a gene, an engineering bacterium and application. The amino acid sequence of the carbonyl reductase mutant is shown as SEQ ID NO: 1, the catalytic efficiency of asymmetric reductive hydrogenation of prochiral ketone compounds is improved, the stereoselectivity of chiral hydroxyl compounds formed through catalysis is improved, and the synthesis efficiency of (S)-1-(5-fluoro-2-iodophenyl) ethanol is improved.