20 results about "High specific activity" patented technology

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 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.

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 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.

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 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 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 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.

The present application relates to the field of genetic engineering and protein modification technology, and particularly relates to a high specific activity basic xylanase mutant and application thereof. The present application takes wild type xylanase H1 as a basis, and provides a mutant containing at least one of the following mutation sites: I37V, A59S, D63E, D104Y, T107M / K, N167G and D192E. Compared with the wild type xylanase H1, the specific activity of the xylanase mutant provided by the present application is generally increased by 8.5%-32.8%; wherein the specific activity of the xylanase mutant containing the D192E single point mutation is the highest, reaching 1625.11 U / mg, which is conducive to reducing the production cost of the enzyme and promoting its wide application in the industrial field.

The invention relates to the technical field of gene engineering and protein engineering, in particular to a high-specific-activity xylanase mutant and application thereof. Compared with wild type xylanase, the specific activity of the xylanase mutant provided by the invention is generally improved by 17.3%-27.6%; wherein the specific activity of the xylanase mutant containing V263M single-point mutation is highest and reaches 1457 U / mg, so that the production cost of the xylanase is reduced, and wide application of the xylanase mutant in the industrial field, especially the field of bio-refinery, is promoted.

The invention discloses an inositol oxidase mutant as well as a preparation method and application thereof, and relates to the technical field of biology, and the mutant is obtained by carrying out common mutation on the 219th site, the 110th site and the 246th site on an inositol oxidase amino acid sequence as shown in SEQ ID NO.1. The synergistic mutation of the three sites effectively changes the local microenvironment or structural rigidity of the enzyme, so that the thermal stability, pH stability and operation stability of zymoprotein are remarkably improved, and meanwhile, the affinity or catalytic turnover rate of the zymoprotein with substrate inositol is enhanced. Compared with a wild type or single / double mutant, the half-life period of the three mutants provided by the invention is obviously prolonged under the actual application condition on the premise of keeping high specific activity, and a key foundation is laid for constructing a reusable immobilized catalyst.

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 invention relates to an anti-autotomy and high-specific-activity AspN enzyme mutant as well as a coding gene and application thereof. The invention aims to solve the problems that the wild type AspN enzyme is easy to self-dissect and inactivate and is poor in stability. The mutant is obtained by mutating one or more aspartic acid sites in the 94th site, the 108th site, the 132 site, the 141 site, the 182 site and the 184 site on the basis of an amino acid sequence shown in SEQ ID NO: 1. The preferred mutations include D182N, D182A, D182V, D132N, D132Q, D184E, D94G, D108T, D141G, and a combination of D182N and D132N. Compared with a wild type, the specific activity and / or the enzyme activity retention rate of the mutant are / is remarkably improved. The stability and catalytic efficiency of the AspN enzyme are effectively improved, and the method has good application prospects in protein sequencing, polypeptide preparation and mass spectrometry.