44 results about "High specific activity" patented technology

The invention relates to the technical field of agricultural biology, in particular to a high-activity multi-copper oxidase mutant V286N and application thereof in mycotoxin degradation. The amino acid sequence of the multi-copper oxidase mutant is as shown in SEQ ID NO: 2. The multi-copper oxidase mutant provided by the invention has higher specific activity. Compared with wild type multi-copper oxidase, the multi-copper oxidase mutant MCO-V286N provided by the invention has the advantages that the specific activity is improved by 0.8 time, the degradation efficiency on mycotoxin zearalenone is improved by 0.4 time, the production and application cost is effectively reduced, and the multi-copper oxidase mutant MCO-V286N has important application value and technical significance in wide application of the multi-copper oxidase in the field of mycotoxin detoxification of food and feed.

The invention belongs to the technical field of genetic engineering and protein engineering modification, and particularly relates to a high-specific-activity cellulase mutant and application thereof. Compared with wild cellulase, the specific activity of the mutant is improved by 51.9% and reaches 319 U / mg, and an unexpected technical effect is achieved. The mutant can be widely applied to the field of textile industry, is uniform in flower formation, small in flower point and strong in stereoscopic impression, most importantly, the strength loss of the fabric is very small, the strength retention rate is improved by 10-15% compared with that of the fabric treated by wild type cellulase, the use amount of the cellulase can be greatly reduced, the cost is reduced, and the application prospect is wide.

Provided are high-specific-activity cellulase mutants and use thereof. Compared to the wild-type cellulase, the specific activity of the provided mutants that comprise single mutation sites P14A, P19T, S75A, S109N, H118P, M123I, M123L, I130L, I130Q, Y167E, Y167F, Y167W, A176S, A176F, D177S, and L192I, respectively, under neutral conditions is generally increased by 10.4% to 76.1%. The single-point mutant comprising I130L has the highest specific activity, which reaches 183.64 U / mg. The production costs of the cellulase mutants are significantly lower, which facilitates the wide use thereof.

Compositions comprising high levels of high specific activity copper-64, and process for preparing said compositions. The compositions comprise from about 2 Ci to about 15 Ci of copper-64 and have specific activities up to about 3800 mCi copper-64 per microgram of copper. The processes for preparing said compositions comprise bombarding a nickel-64 target with a low energy, high current proton beam, and purifying the copper-64 from other metals by a process comprising ion exchange chromatography or a process comprising a combination of extraction chromatography and ion exchange chromatography.

Compositions comprising high levels of high specific activity copper-64, and process for preparing said compositions. The compositions comprise from about 2 Ci to about 15 Ci of copper-64 and have specific activities up to about 3800 mCi copper-64 per microgram of copper. The processes for preparing said compositions comprise bombarding a nickel-64 target with a low energy, high current proton beam, and purifying the copper-64 from other metals by a process comprising ion exchange chromatography or a process comprising a combination of extraction chromatography and ion exchange chromatography.

The application discloses a kind of high specific activity alpha-galactosidase mutant and application thereof.The alpha-galactosidase AgaV derived from Anoxybacillus vitaminiphilus is used as template, amino acid mutation is carried out by using molecular biology technology, a kind of mutant with improved catalytic efficiency is obtained, including A55N, G530C, P579Y and N580Q.The mutant has high catalytic efficiency, and the efficiency of catalyzing synthesis of ectocarpin with D-galactose and glycerol as substrates is improved by 1.5-2.0 times, which is beneficial to reduce the cost of ectocarpin synthesis, improve the conversion efficiency of using the enzyme to produce ectocarpin, and has wide application prospect.

The present application relates to the technical field of genetic engineering and protein modification, and particularly relates to a cellulase mutant with improved specific activity and application thereof. The cellulase mutant has higher specific activity under the condition of 50 DEG C. Compared with the wild type, the specific activity of the cellulase mutant provided by the present application, which respectively contains N60Q, L78V, A92E, N124Q, M125I, Q169E, Q187R, S230G, D239A single-point mutations, is generally increased by 8.6%-35.7% under the condition of 50 DEG C. Among them, the specific activity of the L78V single-point mutant and the N124Q single-point mutant is increased by 30% and 35.7% respectively, thereby facilitating the wide application of the cellulase in the textile field.

The invention relates to the technical field of genetic engineering and protein engineering modification, in particular to a high-specific-activity alkaline protease mutant. According to the invention, on the basis of wild type alkaline protease AprE from bacillus clausii, a mutant containing mutation sites selected from the group consisting of V30I, I77L, I77V, S101G, N138Q, N138K, F183D, V197I, V197L, P219W, P219E, A226G and A226T is provided. The specific activity of the mutant is remarkably improved, the production cost of the enzyme is reduced, and wide application of the enzyme in the field of washing industry is promoted.

The present application relates to the field of agricultural biotechnology, and in particular to a high-activity multicopper oxidase mutant V286N and its application in mycotoxin degradation. The amino acid sequence of the multicopper oxidase mutant is shown as SEQ ID NO: 2. The multicopper oxidase mutant provided by the present application has higher specific activity. Compared with the wild-type multicopper oxidase, the specific activity of the multicopper oxidase mutant MCO-V286N provided by the present application is increased by 0.8 times, the degradation efficiency of mycotoxin zearalenone is increased by 0.4 times, the production and application cost is effectively reduced, and the multicopper oxidase has important application value and technical significance for the wide application of the multicopper oxidase in the field of mycotoxin detoxification of food and feed.

The invention relates to the technical field of genetic engineering and protein engineering modification, in particular to a high-specific-activity alkaline protease mutant. According to the invention, on the basis of wild type alkaline protease AprE from bacillus clausii, a mutant containing mutation sites selected from the group consisting of V30I, I77L, I77V, S101G, N138Q, N138K, F183D, V197I, V197L, P219W, P219E, A226G and A226T is provided. The specific activity of the mutant is remarkably improved, the production cost of the enzyme is reduced, and wide application of the enzyme in the field of washing industry is promoted.

The present application relates to the technical field of genetic engineering and protein modification, and particularly relates to a high specific activity cellulase mutant and application thereof. The mutant provided by the present application comprises substitution of amino acids at at least one position selected from the group consisting of 44, 84, 109, 123, 178, 183, 194, 225 and 234. The specific activity of the mutant at 50 DEG C is generally increased by 7.1% to 38%; wherein the specific activity of the S44N single-point mutant, the I123L single-point mutant and the L194I single-point mutant is respectively increased by 26.8%, 25.7% and 38%, thereby facilitating the wide application of the cellulase in the textile field.

The present application relates to the technical field of genetic engineering and protein modification, and particularly relates to a high specific activity cellulase mutant and application thereof. The mutant provided by the present application comprises substitution of amino acids at at least one position selected from the group consisting of 44, 84, 109, 123, 178, 183, 194, 225 and 234. The specific activity of the mutant at 50 DEG C is generally increased by 7.1% to 38%; wherein the specific activity of the S44N single-point mutant, the I123L single-point mutant and the L194I single-point mutant is respectively increased by 26.8%, 25.7% and 38%, thereby facilitating the wide application of the cellulase in the textile field.

The present disclosure is directed compositions and formulations comprising high levels of high specific activity copper-64, and process for preparing said compositions. The compositions comprise from about 2 Ci or greater of copper-64 and have specific activities up to about 3850 mCi copper-64 per microgram of copper. The processes for preparing said compositions comprise bombarding a nickel-64 target with a low energy, high current proton beam, and purifying the copper-64 from other metals by a process comprising ion exchange chromatography or a process comprising a combination of extraction chromatography and ion exchange chromatography.

This application belongs to the field of genetic engineering technology and discloses human enterokinase light chain mutants and their applications. This application involves single-point mutations or multiple rounds of combined mutations based on the wild-type human enterokinase light chain -C112S mutant sequence. The obtained variants have higher specific activity compared to the parent, which is expected to increase unit yield, reduce the residual amount of protease in the final product, and lower product costs. Furthermore, these mutants exhibit high stability in the enzymatic digestion of peptides / proteases, such as liraglutide and smegglutide, GLP-1 analogs, reducing enzyme usage, increasing digestion efficiency, and decreasing the proportion of non-specific products, thereby lowering the production cost of peptide drugs and promoting the rapid development of related industries.

The invention belongs to the technical field of biology, and particularly relates to a carboxypeptidase B (CPB) precursor gene sequence, a recombinant carboxypeptidase B precursor and a preparation method of carboxypeptidase B. The gene sequence of the carboxypeptidase B precursor is as shown in SEQ ID No.6, the amino acid sequence of the carboxypeptidase B precursor is as shown in SEQ ID No.5, the gene sequence of the CPB enzyme target gene is as shown in SEQ ID No.2, and the amino acid sequence of the CPB enzyme target gene is as shown in SEQ ID No.4. The preparation method of the CPB comprises the following steps: (1) cloning and constructing a CPB enzyme expression vector; (2) expressing CPB precursor protein by using engineering bacteria to form an inclusion body; (3) thalli are washed, crushed and centrifuged, inclusion bodies are collected, and denatured dissolution is performed; (4) inclusion body renaturation; and (5) activating and purifying CPB. The process is simple and convenient in steps, does not use animal pancreas, and reduces the possibility of infection; the obtained CPB enzyme has high specific activity, and the yield of each liter of fermentation liquor is high, so that the method is suitable for large-scale production and application.

The present application relates to the technical field of genetic engineering and protein modification, and particularly relates to a high specific activity cellulase mutant and application thereof. The mutant provided by the present application comprises substitution of amino acids at at least one position selected from the group consisting of 44, 84, 109, 123, 178, 183, 194, 225 and 234. The specific activity of the mutant at 50 DEG C is generally increased by 7.1% to 38%; wherein the specific activity of the S44N single-point mutant, the I123L single-point mutant and the L194I single-point mutant is respectively increased by 26.8%, 25.7% and 38%, thereby facilitating the wide application of the cellulase in the textile field.

The present invention provides a detergent composition containing α-amylase that exhibits high specific activity at low temperatures. [Solution] A detergent composition containing one or more proteins selected from (A), (B), (C), and (D) below. (A) A protein having an amino acid sequence that is at least 90% identical to the amino acid sequence shown in Sequence ID No. 2, and which also has α-amylase activity. (B) A protein having an amino acid sequence that is at least 90% identical to the amino acid sequence shown in Sequence ID No. 4, and which also has α-amylase activity. (C) A protein having an amino acid sequence that is at least 90% identical to the amino acid sequence shown in Sequence ID No. 6, and which also has α-amylase activity. (D) A protein having an amino acid sequence that is at least 90% identical to the amino acid sequence shown in Sequence ID No. 8, and which also has α-amylase activity.

The present application relates to the technical field of genetic engineering and protein engineering, and particularly relates to a xylanase mutant. The mutant is a single-point mutant provided based on wild-type xylanase Xyn, and the specific activity of the mutant is generally increased by 12.4%-63.4%. The xylanase mutant containing the I128E single-point mutation has the highest specific activity of 1273.9 U / mg, which is conducive to reducing the production cost of the enzyme and promoting the wide application of the enzyme in the feed field.

The present application relates to the technical field of enzyme engineering, and particularly relates to a high specific activity halophilic proarchibacter alkaline phosphatase and application thereof.The high specific activity halophilic proarchibacter alkaline phosphatase has a sequence as shown in SEQ ID NO.2, is a low-cost, high-specific-activity alkaline phosphatase, the specific activity of which is 48.41 times that of Escherichia coli alkaline phosphatase EAP and 1.69 times that of bovine small intestine alkaline phosphatase BIAP.The high specific activity halophilic proarchibacter alkaline phosphatase can be used for labeling antibodies and small molecule antigens.

The application relates to the technical field of genetic engineering and protein modification, and particularly relates to a lipase mutant and application of the lipase mutant in oil processing. Compared with a wild-type lipase RL, the specific activity of the lipase mutant provided by the application is increased by 97.9%, reaching 5753 U / mg, and an unexpected technical effect is achieved. The lipase mutant has higher specific activity, which is beneficial to reducing the production cost of the lipase mutant and promoting the wide application of the lipase mutant in the field of oil processing and the like.

This invention discloses an apparatus and method for preparing a high specific activity Tb-161 solution, belonging to the field of radioisotope preparation technology. It includes: a shielded box and a target material processing system, a separation system, a radioactivity detection system, and a control system housed within the shielded box. The separation system is used to adsorb the target material solution, elute it with an organic carboxylic acid eluent, and process the obtained Tb-161-containing eluent to obtain a Tb-161-containing solution. The apparatus for preparing a high specific activity Tb-161 solution provided by this invention separates Tb-161 from irradiated Gd-160-enriched target material using ion chromatography, significantly improving the yield and specific activity of terbium-161 and simplifying the separation process. The constant column temperature during separation greatly reduces waste liquid volume, shortens separation time, and avoids the problem of insufficient terbium-161 specific activity caused by gadolinium tailing.

The present application relates to the field of enzyme engineering, and in particular to a method for improving the catalytic activity of alpha-glucan phosphorylase and a mutant Tp Alpha-glucan phosphorylase, genes and applications. In order to simultaneously meet the excellent thermal stability required for high-temperature operation and the high specific activity required for efficient catalysis of existing alpha-glucan phosphorylases, the present application uses site-directed mutagenesis technology to modify alpha-glucan phosphorylase from Thermotoga petrophila Thermus thermophilus HB27, and obtain a single-point mutant with improved catalytic activity Tp Alpha-glucan phosphorylase. The alpha-glucan phosphorylase mutant of the present application can be widely used in the production of artificial starch and other polysaccharides.

The present application relates to the technical field of genetic engineering and protein engineering, and particularly relates to a high specific activity alkaline protease mutant. The mutant contains at least one mutation site selected from Q63K, A109T, K120N, G154W, G191V, A261L and T328G. The specific activity of the mutant is obviously higher than that of wild type alkaline protease, which is beneficial to reduce the production cost of the enzyme and promote its wide application in the field of industrial enzymes.

The present application relates to the field of agricultural biotechnology, and particularly relates to a beta-1,3-glucanase mutant N54W and a gene and application thereof. The amino acid sequence of the beta-1,3-glucanase N54W mutant is shown as SEQ ID NO:2. Compared with the wild-type beta-1,3-glucanase, the specific activity of the beta-1,3-glucanase mutant is increased by 3.6 times, reaches 902.1 U / mg, the catalytic activity is greatly improved, k cat / K m reaches 888.9 ml·mg ‑1 ·min ‑1 , reaches 5.5 times of the wild type. The present application provides the application of the beta-1,3-glucanase mutant with high specific activity, and the beta-1,3-glucanase mutant can be particularly applied in brewing, food and feed fields, and has a very broad application prospect.

Compositions comprising high levels of high specific activity copper-64, and process for preparing said compositions. The compositions comprise from about 2 Ci to about 15 Ci of copper-64 and have specific activities up to about 3800 mCi copper-64 per microgram of copper. The processes for preparing said compositions comprise bombarding a nickel-64 target with a low energy, high current proton beam, and purifying the copper-64 from other metals by a process comprising ion exchange chromatography or a process comprising a combination of extraction chromatography and ion exchange chromatography.

The present application relates to the field of genetic engineering and protein engineering, and particularly relates to a high specific activity alkaline xylanase mutant. The present application provides a mutant containing H61L mutation site based on wild type xylanase H1. The specific activity of the mutant is significantly higher than that of the wild type, which is beneficial to reduce the production cost and promote its wide application in the industrial field.

The invention relates to the technical field of gene engineering and protein engineering, in particular to a glucanase mutant with high antibacterial activity and high specific activity and heat resistance and application of the glucanase mutant. According to the invention, 1, 3-1, 4-beta-glucanase Feglc16A is taken as a female parent, and a combined mutant M4 is screened through a directed evolution technology. In the aspect of thermal stability, the T50 value and the half-life period at 60 DEG C of the mutant M4 are respectively improved by 9 DEG C and 62 minutes compared with those of a wild enzyme; in the aspect of enzyme activity, the specific activity and the catalytic efficiency of the mutant M4 are respectively increased by 54% and 142% compared with those of a wild enzyme; in the aspect of antibacterial performance, the antibacterial rates of the mutant M4 on aspergillus niger and aspergillus flavus are respectively improved by 44% and 53%. The acquisition of the heat-resistant glucanase mutant M4 with high catalytic efficiency provides reference for the improvement of the catalytic performance of the glucanase, and the mutant M4 with excellent antibacterial performance shows huge application prospects in the production of green antibacterial agents.

The application discloses a kind of alpha-galactosidase mutants with high specific activity and thermal stability and application thereof.The alpha-galactosidase AgaV derived from Anoxybacillus vitaminiphilus is used as a template, and amino acid mutation is carried out by using molecular biology techniques to obtain a kind of mutant with improved catalytic efficiency, including Y340E, N549Q and T550N.The mutant has high catalytic efficiency and strong thermal stability, and the hydrolysis efficiency of rfo, such as raffinose and stachyose, is increased by 4.0-6.0 times, and has a wide application prospect for hydrolysis and removal of rfo in soybean products.

The invention relates to the field of synthetic biology and fermentation engineering, and discloses a preparation method and application of high-specific-activity phenylalanine ammonialyase cells, and the preparation method comprises the following steps: in a cell growth period, adopting a DO-stat feeding strategy fed back by a dissolved oxygen concentration, and monitoring and controlling the acetic acid concentration to be below a preset threshold value in a linkage manner, so as to obtain high-specific-activity phenylalanine ammonialyase cells; the inhibition of overflow metabolism on cell growth is avoided; and after the cells reach a preset high density, target protein expression is induced under a low-temperature condition. The obtained cell is used as a whole-cell catalyst, or after being immobilized, the cell is used for catalyzing deamination of L-phenylalanine to efficiently synthesize trans-cinnamic acid. According to the method disclosed by the invention, the contradiction between high-density culture and high-activity expression is solved through a coordinated regulation strategy, and the obtained cell catalyst has the characteristics of high thallus density and strong enzyme specific activity, and shows the beneficial effects of high conversion rate, good product purity, strong stability after immobilization and repeated recycling in catalytic application.

The application belongs to the technical field of genetic engineering and protein engineering modification, and particularly relates to a high specific activity cellulase mutant and application thereof. Compared with wild type cellulase, the specific activity of the mutant is increased by 51.9%, reaches 319 U / mg, and unexpected technical effects are achieved. The mutant can be widely applied to the field of textile industry, has uniform raising, small flower points, strong stereoscopic feeling, and most importantly, has particularly small fabric strength loss, the fabric strength retention rate of the mutant is increased by 10%-15% compared with that of the wild type cellulase, the cellulase usage can be greatly reduced, the cost is reduced, and the mutant has wide application prospect.