41 results about "Glucose dehydrogenase" patented technology

The invention belongs to the field of metabolic engineering, and discloses a genetically engineered bacterium for producing myo-inositol as well as a construction method and application of the genetically engineered bacterium. The genetically engineered bacterium takes escherichia coli as an original strain, and is obtained by performing the following gene editing on a genome of the escherichia coli: non-expressed lactose operon repressor protein, glucose phosphate dehydrogenase, acetokinase, glucose phosphate isomerase and glycerol repressor protein; and overexpressing inositol-1-phosphate synthase, inositol monophosphate, glucokinase, glucose permease and glycerol kinase. Compared with the prior art, the genetically engineered bacterium disclosed by the invention has remarkable advantages in the aspects of key enzyme expression rate, metabolism specificity, fermentation period and the like, and an efficient, stable, economical and feasible solution is provided for industrial production of myo-inositol.

The invention discloses a genetically engineered bacterium for producing heparinogen and a construction method and application thereof, the genetically engineered bacterium takes Escherichia coli Nissle 1917 as a chassis bacterium, and the construction method comprises the following steps: (1) knocking out endonuclease I coding gene endA in a chassis bacterium genome; (2) knocking out a 6-phosphofructokinase I coding gene pfkA in a chassis bacterium genome; (3) carrying out overexpression on a 6-phosphoglucosamine synthetase encoding gene glmS and / or a UDP-glucose-6-dehydrogenase encoding gene kfiD from a chassis bacterium genome; (4) removing the feedback inhibition of the 6-phosphate glucosamine on the GlmS so as to promote the synthesis of UDP-N-acetylglucosamine; and (5) knocking out the 6-phosphate glucosamine deaminase coding gene nagB in the chassis bacterium genome. The engineering strain obtained by the invention can more efficiently synthesize the proheparin, the shake flask titer reaches 397.9 mg / L, which is increased by about 3 times compared with a wild strain, and the engineering strain has certain industrial application value.

This application relates to a phenytoin detection kit. Specifically, the glucose-6-phosphate dehydrogenase mutant of this application contains one mutation selected from the following compared to the wild-type glucose-6-phosphate dehydrogenase: D306C, D375C, or G426C. The detection kit prepared using the glucose-6-phosphate dehydrogenase mutant of this application exhibits high specificity, high sensitivity, ease of operation, short detection time, and accurate quantification, making it suitable for high-throughput detection.

The present application relates to a preparation method of a conjugate. Specifically, the 6-phosphogluconate dehydrogenase mutant of the present application comprises one mutation or a combination thereof selected from D306C, D375C, G426C compared with wild-type 6-phosphogluconate dehydrogenase. The detection kit prepared by using the 6-phosphogluconate dehydrogenase mutant of the present application has high specificity, high sensitivity, convenient operation, short detection time, accurate quantification, and is suitable for high-throughput detection.

The present application relates to a methotrexate detection kit. Specifically, the 6-phosphogluconate dehydrogenase mutant of the present application comprises one mutation or a combination thereof selected from the following: D306C, D375C, G426C, compared with wild-type 6-phosphogluconate dehydrogenase. The detection kit prepared using the 6-phosphogluconate dehydrogenase mutant of the present application has strong specificity, high sensitivity, convenient operation, short detection time, accurate quantification, and is suitable for high-throughput detection.

This application relates to the use of conjugates in the preparation of diagnostic reagents. Specifically, the glucose-6-phosphate dehydrogenase mutant of this application contains one or a combination of mutations selected from the following, compared to the wild-type glucose-6-phosphate dehydrogenase: D306C, D375C, and G426C. Diagnostic kits prepared using the glucose-6-phosphate dehydrogenase mutant of this application exhibit high specificity, high sensitivity, ease of operation, short detection time, and accurate quantification, making them suitable for high-throughput detection.

This application relates to the use of conjugates in the preparation of diagnostic reagents. Specifically, the glucose-6-phosphate dehydrogenase mutant of this application contains one or a combination of mutations selected from the following, compared to wild-type glucose-6-phosphate dehydrogenase: D306C, D375C, and G426C. Diagnostic kits prepared using the glucose-6-phosphate dehydrogenase mutant of this application exhibit high specificity, high sensitivity, ease of operation, short detection time, and accurate quantification, making them suitable for high-throughput detection.

The present application relates to a preparation method of a conjugate. Specifically, the 6-phosphogluconate dehydrogenase mutant of the present application comprises one mutation or a combination thereof selected from D306C, D375C, G426C compared with wild-type 6-phosphogluconate dehydrogenase. The detection kit prepared by using the 6-phosphogluconate dehydrogenase mutant of the present application has high specificity, high sensitivity, convenient operation, short detection time, accurate quantification, and is suitable for high-throughput detection.

This application relates to a digoxin detection kit. Specifically, the 6-glucose phosphate dehydrogenase mutant of this application comprises one or a combination of the following mutations compared to wild-type 6-glucose phosphate dehydrogenase: D306C, D375C, and G426C. The detection kit prepared using the 6-glucose phosphate dehydrogenase mutant of this application has strong specificity, high sensitivity, convenient operation, short detection time, and accurate quantitative determination, making it suitable for high-throughput detection.

The application relates to a digitalis glycoside detection kit. Specifically, the 6-phosphogluconate dehydrogenase mutant of the application comprises one mutation or a combination thereof selected from D306C, D375C, G426C compared with wild-type 6-phosphogluconate dehydrogenase. The detection kit prepared by using the 6-phosphogluconate dehydrogenase mutant of the application has the advantages of high specificity, high sensitivity, convenient operation, short detection time, accurate quantification and suitability for high-throughput detection.

The invention belongs to the technical field of biochemical energy batteries, and discloses an implantable biochemical energy battery array, a chip and application. Comprising a plurality of biochemical energy power generation units which are mutually connected through a microfluidic channel to form a biochemical energy power generation array, the power generation array is connected in series and in parallel to form a battery array, and glucose fluid flows through the microfluidic channel. The power generation unit comprises a positive electrode, a biochemical decomposition chamber and a negative electrode, carrier materials of hexokinase HK, glucose 6-phosphate dehydrogenase G6PD, glucose 6-phosphate lactonase PGLS and glucose 6-phosphate dehydrogenase 6PGDH are fixed in the biochemical decomposition chamber, and the negative electrode is coated with an artificial film assembled with NADPH transhydrogenase and mitochondrial respiratory chain compound protein. According to the invention, glucose is used as fuel of the cell for continuous power generation, and the flexible array biochemical energy cell which is miniaturized, high in load, long in endurance, capable of being shaped and high in energy density can be provided.

This application relates to the use of conjugates in the preparation of diagnostic reagents. Specifically, the glucose-6-phosphate dehydrogenase mutant of this application contains one or a combination of mutations selected from the following, compared to wild-type glucose-6-phosphate dehydrogenase: D306C, D375C, and G426C. Diagnostic kits prepared using the glucose-6-phosphate dehydrogenase mutant of this application exhibit high specificity, high sensitivity, ease of operation, short detection time, and accurate quantification, making them suitable for high-throughput detection.

This application relates to a method for preparing a conjugate. Specifically, the 6-glucose phosphate dehydrogenase mutant of this application comprises one or a combination of the following mutations compared to wild-type 6-glucose phosphate dehydrogenase: D306C, D375C, and G426C. The detection kit prepared using the 6-glucose phosphate dehydrogenase mutant of this application has strong specificity, high sensitivity, convenient operation, short detection time, and accurate quantitative determination, making it suitable for high-throughput detection.

This application relates to a gentamicin detection kit. Specifically, the 6-glucose phosphate dehydrogenase mutant described herein comprises one or a combination of the following mutations compared to wild-type 6-glucose phosphate dehydrogenase: D306C, D375C, and G426C. The gentamicin detection kit prepared using the 6-glucose phosphate dehydrogenase mutant described herein has strong specificity, high sensitivity, ease of use, short detection time, and minimal inter-batch variability, and has promising application prospects.

This application relates to a method for preparing conjugates. Specifically, the glucose-6-phosphate dehydrogenase mutant of this application contains one or a combination of mutations selected from the following, compared to the wild-type glucose-6-phosphate dehydrogenase: D306C, D375C, and G426C. The detection kit prepared using the glucose-6-phosphate dehydrogenase mutant of this application exhibits high specificity, high sensitivity, ease of operation, short detection time, and accurate quantification, making it suitable for high-throughput detection.

The application discloses high-yield gernien A engineering methanotrophs, a construction method and application thereof, and belongs to the technical field of metabolic engineering and synthetic biology. P mxaF expressing a gernien A synthase encoding gene gas overexpressing a 1-deoxy-xylose-5-phosphate synthase encoding gene in a gernien A synthesis pathway dxs1 and dxs2 a farnesyl pyrophosphate synthase encoding gene ispA a isopentenyl pyrophosphate isomerase encoding gene Bsidi simultaneously overexpressing 6-phosphogluconate dehydrogenase zwf1 and pfk1 and fba2 in an EMP pathway, to obtain gernien A engineering methanotrophs. The fermentation production of gernien A is carried out by using the engineering methanotrophs, and the yield of gernien A is obviously improved, so that the engineering methanotrophs have an industrial application prospect.

The application relates to a preparation method of a conjugate. Specifically, the 6-phosphogluconate dehydrogenase mutant of the application comprises one mutation or a combination thereof selected from D306C, D375C, G426C compared with wild-type 6-phosphogluconate dehydrogenase. The detection kit prepared by using the 6-phosphogluconate dehydrogenase mutant of the application has the advantages of high specificity, high sensitivity, convenient operation, short detection time, accurate quantification and suitability for high-throughput detection.

This application relates to the use of conjugates in the preparation of reagent kits. Specifically, the glucose-6-phosphate dehydrogenase mutant of this application contains a mutation selected from one or a combination of the following, compared to the wild-type glucose-6-phosphate dehydrogenase: D306C, D375C, and G426C. Gentamicin detection kits prepared using the glucose-6-phosphate dehydrogenase mutant of this application exhibit high specificity, high sensitivity, ease of operation, short detection time, and small batch-to-batch variation, demonstrating promising application prospects.

This application relates to the use of conjugates in the preparation of phenytoin detection reagents. Specifically, the 6-glucose phosphate dehydrogenase mutant of the present application comprises one of the following mutations, D306C, D375C, and G426C, compared to wild-type 6-glucose phosphate dehydrogenase. The detection kit prepared using the 6-glucose phosphate dehydrogenase mutant of the present application has strong specificity, high sensitivity, convenient operation, short detection time, and accurate quantitative determination, making it suitable for high-throughput detection.

The application relates to a preparation method of a gentamicin detection reagent. Specifically, a 6-phosphogluconate dehydrogenase mutant of the application comprises one mutation or a combination thereof selected from D306C, D375C and G426C compared with wild-type 6-phosphogluconate dehydrogenase. A gentamicin detection kit prepared by using the 6-phosphogluconate dehydrogenase mutant of the application has the advantages of high specificity, high sensitivity, convenient operation, short detection time, small batch difference and good application prospect.

This invention discloses an engineered methanogenic bacterium that produces high levels of squalene, its construction method, and its applications, belonging to the fields of metabolic engineering and synthetic biology. This is achieved by using a strong promoter in the host bacterium (methanogenic bacterium). P mxaF Expression of squalene synthase encoding gene sqs Overexpression of the gene encoding 1-deoxy-xylulose-5-phosphate synthase in the squalene synthesis pathway dxs1 and dxs2 Farnesyl pyrophosphate synthase encoding gene ispA Isopentenyl pyrophosphate isomerase encoding gene My friends Simultaneously overexpressing glucose-6-phosphate dehydrogenase zwf1 and the EMP pathway pfk1 and fba2 An engineered methanogenic bacterium producing squalene was obtained. Using this engineered methanogenic bacterium for squalene fermentation production can significantly increase squalene yield and has excellent prospects for industrial application.

The present application relates to a preparation method of a conjugate. Specifically, the 6-phosphogluconate dehydrogenase mutant of the present application comprises one mutation or a combination thereof selected from D306C, D375C, G426C compared with wild-type 6-phosphogluconate dehydrogenase. The detection kit prepared by using the 6-phosphogluconate dehydrogenase mutant of the present application has high specificity, high sensitivity, convenient operation, short detection time, accurate quantification, and is suitable for high-throughput detection.

The application relates to a preparation method of a conjugate. Specifically, the 6-phosphogluconate dehydrogenase mutant of the application comprises one mutation selected from D306C, D375C and G426C compared with wild-type 6-phosphogluconate dehydrogenase. The detection kit prepared by using the 6-phosphogluconate dehydrogenase mutant of the application is high in specificity, high in sensitivity, convenient to operate, short in detection time, accurate in quantification and suitable for high-throughput detection.

This application relates to the use of conjugates in the preparation of diagnostic reagents. Specifically, the glucose-6-phosphate dehydrogenase mutant of this application contains one or a combination of mutations selected from the following, compared to wild-type glucose-6-phosphate dehydrogenase: D306C, D375C, and G426C. Diagnostic kits prepared using the glucose-6-phosphate dehydrogenase mutant of this application exhibit high specificity, high sensitivity, ease of operation, short detection time, and accurate quantification, making them suitable for high-throughput detection.

This application relates to a vancomycin detection kit. Specifically, the 6-glucose phosphate dehydrogenase mutant of the present application comprises one or a combination of the following mutations compared to wild-type 6-glucose phosphate dehydrogenase: D306C, D375C, and G426C. The detection kit prepared using the 6-glucose phosphate dehydrogenase mutant of the present application has strong specificity, high sensitivity, convenient operation, short detection time, and accurate quantitative determination, making it suitable for high-throughput detection.

This application relates to a tacrolimus detection kit. Specifically, the glucose-6-phosphate dehydrogenase mutant of this application contains one or a combination of mutations selected from the following, compared to the wild-type glucose-6-phosphate dehydrogenase: D306C, D375C, and G426C. The detection kit prepared using the glucose-6-phosphate dehydrogenase mutant of this application exhibits high specificity, high sensitivity, ease of operation, short detection time, and accurate quantification, making it suitable for high-throughput detection.

This application relates to an amikacin detection kit. Specifically, the glucose-6-phosphate dehydrogenase mutant of this application contains one or a combination of mutations selected from the following, compared to the wild-type glucose-6-phosphate dehydrogenase: D306C, D375C, and G426C. The detection kit prepared using the glucose-6-phosphate dehydrogenase mutant of this application exhibits high specificity, high sensitivity, ease of operation, short detection time, and accurate quantification, making it suitable for high-throughput detection.

This application relates to the use of conjugates in the preparation of detection reagents. Specifically, the 6-glucose phosphate dehydrogenase mutant of the present application comprises one or a combination of the following mutations compared to wild-type 6-glucose phosphate dehydrogenase: D306C, D375C, and G426C. The detection kit prepared using the 6-glucose phosphate dehydrogenase mutant of the present application has strong specificity, high sensitivity, convenient operation, short detection time, and accurate quantitative determination, making it suitable for high-throughput detection.

The present application relates to a preparation method of a conjugate. Specifically, the 6-phosphogluconate dehydrogenase mutant of the present application comprises one mutation or a combination thereof selected from D306C, D375C, G426C compared with wild-type 6-phosphogluconate dehydrogenase. The detection kit prepared by using the 6-phosphogluconate dehydrogenase mutant of the present application has high specificity, high sensitivity, convenient operation, short detection time, accurate quantification, and is suitable for high-throughput detection.

The invention discloses a drug target protein Ugd and application thereof in agriculture, and relates to the technical field of agricultural biology. The UDP glucose 6-dehydrogenase protein (Ugd) is identified from sclerotium rolfsii and fusarium graminearum through target stability analysis of a drug affinity reaction by taking a plant source natural product butenyl phthalide as a probe; according to the application disclosed by the invention, the Ugd protein is identified as a potential action target of butenyl phthalide for the first time, functional domains of the Ugd protein in sclerotium rolfsii and fusarium graminearum are defined, amino acids at the 371-466th sites of the fusarium graminearum Ugd protein form an important functional domain, amino acids at the 336-452 sites of the sclerotium rolfsii Ugd protein form a key functional domain, and the Ugd protein is identified as the potential action target of butenyl phthalide. The functional domains can be used as specific receptor sites for designing targeted drugs, and the drugs specifically bound with the Ugd protein can be accurately designed according to molecular structure characteristics of the functional domains and the structural domains through technologies such as molecular docking and the like.