8 results about "Hydrolase Gene" patented technology

The invention discloses recombinant xanthomonas campestris with xanthan gum hydrolase displayed on the surface and a construction method and application of the recombinant xanthomonas campestris. The recombinant xanthomonas campestris for surface display of xanthan hydrolase is constructed by introducing a recombinant vector obtained by fusion expression of an ice crystal nuclein (INP) gene and a xanthan hydrolase gene into xanthomonas campestris. The gel yield of recombinant xanthomonas campestris fermentation is twice that of a wild strain and reaches 6.7 g / L. The strain can efficiently hydrolyze xanthan gum with high molecular weight (such as more than 100 wDa), the traditional production process which is relatively complicated is simplified, and a new method is provided for large-scale production of the xanthan gum with low molecular weight.

This invention relates to the construction and staining application of recombinant Escherichia coli for synthesizing indoleacetic acid ester. The recombinant Escherichia coli for synthesizing indoleacetic acid ester is obtained by using recombinant Escherichia coli MG1655ΔpheAΔtrpRΔtyrAΔyddGΔarsB::tac70-MaFMOΔldhA::tac70-MaFMOΔyghWX::tac70-tnaAΔpoxB::tac70-cav1 as the initial strain. Then, the endogenous acetylesterase is knocked out, and the endogenous tryptophan hydrolase gene tnaA and the flavin monooxygenase gene maFMO are overexpressed, while simultaneously overexpressing the acetyltransferase gene. The indoleacetic acid ester yield of this invention is as high as 195.3 mg / L. Using indoleacetic acid ester for staining eliminates the need for reducing agents and enzyme solutions, significantly reducing staining costs.

The invention discloses miR-10490-5p for preventing and treating spodoptera frugiperda and application thereof, miR-10490-5p targeting a key gene for growth and development of the spodoptera frugiperda is screened for the first time, and after an analogue agomiR-10490-5p of the miR-10490-5p is injected, it is found that the miR-10490-5p can inhibit normal expression of a juvenile hormone epoxy hydrolase (JHEH) gene of the spodoptera frugiperda, and the miR-10490-5p can inhibit the growth and development of the spodoptera frugiperda. Therefore, the growth and development of the spodoptera frugiperda larvae are slowed down, the feed intake is reduced, and the death rate is increased. In addition, by adding the analogue agomiR-10490-5p into the feed, the growth of the spodoptera frugiperda can be inhibited, the food intake is reduced, and the death rate is increased. The invention provides a new target and technical support for establishing a new strategy for preventing and controlling the spodoptera frugiperda based on the miRNA.

The present invention generally relates to methods of biological reduction of metal-cyanide complexes after metal-cyanidation and methods of biologically hydrolysing cyanide. More particularly, the present invention allows the engineering of an integrated synthetic lixiviant biological system to be housed within a synthetic host (such as the cyanogenic Chromobacterium violaceum) for efficient precious metal recovery and toxic metal remediation of electronic waste; with up to four main components / modules in the design and engineering of the synthetic host: 1) synthetic cyanogenesis; 2) synthetic metal recovery; 3) synthetic cyanolysis; and 4) synthetic circuits for lixiviant biology. Bacteria capable of reducing ionic metal to ionic metal (such as gold or silver) as nanoparticles, comprising mercury(11) reductase (MerA) comprising a substitution mutation at position V317, Y441, C464, A323D, A414E, G415I, E416C, L417I, I418D, or A422N, are also disclosed. Processes of synthetic cyanide lixiviant production using genetically engineered bacterium transformed with a heterologous hydrogen cyanide synthase gene and a heterologous 3-phosphoglycerate dehydrogenase mutant gene are also disclosed. Processes of synthetic cyanolysis using a genetically engineered bacterium transformed with a heterologous nitrilase gene are also disclosed.

This application discloses an epoxide hydrolase gene cloned from Angelica dahurica. AdEH1 and AdEH2 and its encoded proteins and applications, among which, AdEH 1 and AdEH2 The nucleotide sequences are shown in SEQ ID NO: 1 and SEQ ID NO: 2, respectively, and the amino acid sequences encoding the proteins are shown in SEQ ID NO: 3 and SEQ ID NO: 4, respectively. AdEH1 and AdEH2 The encoded protein possesses epoxide hydrolase catalytic activity, capable of catalyzing the oxidation of imperatorin and angelica root to produce hydrated oxidized imperatorin and angelica root. This application identifies the gene. AdEH1 and AdEH2 Its key role in the biosynthesis of furanocoumarins provides core gene resources for the regulation and green large-scale synthesis of furanocoumarin components in Angelica dahurica, and also provides technical support for the accurate detection of related compounds.

This invention provides a group of recombinant *E. coli* strains capable of synthesizing D-allulose, wherein the recombinant *E. coli* strains include the following modifications: (a) introduction and expression of dTDP-glucose-3-epimerase gene, NDP sugar hydrolase gene, allosugar-1 phosphate-isomerase gene, and acid phosphatase gene; (b) enhanced expression of glucose-1-phosphate thymidine transferase gene, glucose-1-phosphate thymidine transferase 1 gene, and glucose-1-phosphate thymidine transferase 2 gene. This disclosure produces recombinant *E. coli* strains capable of high-yield D-allulose production, increasing the yield of the target compound while reducing the yield of by-products, thus solving a bottleneck problem in industrial production and enabling large-scale production of D-allulose.

The application discloses a glycosyl hydrolase, a gene, a carrier, a host cell and an application. The glycosyl hydrolase is (a) or (b): (a) a glycosyl hydrolase with an amino acid sequence shown in SEQ ID NO:1; (b) a glycosyl hydrolase with equivalent functions derived from (a) by replacing, deleting or adding one or more amino acids in the amino acid sequence shown in SEQ ID NO:1. The glycosyl hydrolase of the application can selectively hydrolyze the glucosyl on the 3rd carbon of PPD type ginsenoside.

The invention belongs to the technical field of genetic engineering and biological fermentation, and particularly relates to a genetically engineered bacterium, a construction method and application, the genetically engineered bacterium simultaneously contains a dehydrogenase gene and a hydrolase gene, the dehydrogenase is 3-ketosteroid-delta1-dehydrogenase, the nucleotide sequence of the dehydrogenase gene is SEQ ID No.5, and the corresponding protein sequence is SEQ ID No.6; the hydrolase is esterase, the nucleotide sequence of the hydrolase gene is SEQ ID No.7, and the corresponding protein sequence is SEQ ID No.8; according to the present invention, the enzyme liquid of the genetically engineered bacterium is adopted to convert substrates such as hydrocortisone acetate and 6 alpha-methyl hydrocortisone acetate, the conversion is complete within the high substrate content and the short time, the conversion rate reaches 99%, and the genetically engineered bacterium is suitable for industrial production.