In order to produce chondroitin sulfate in an animal-free manner, engineered E. coli host cells were modified so as to reduce expression of an endogenous gene for fructosyltransferase (kfoE); reduce expression of an endogenous gene for 3′-phosphoadenosine-5′-phosphosulfate reductase (cysH); and express one or more exogenous sulfotransferases. Expression of proteins forming ATP-binding cassette transporters were also reduced to limit export of glycosaminoglycans from the cells. The recombinant microorganisms are able produce all three components identified for chondroitin sulfate production—chondroitin, sulfate donor, and sulfotransferase. These modified E. coli are capable of complete, essentially one-step biosynthesis of chondroitin sulfate at a variety of sulfation levels from simple microbial media components and glucose. This is a major advantage over current production methods that depend on the natural distribution of chondroitin sulfate types in the animal tissue.

The present disclosure provides a group of novel uridine diphosphate (UDP)-glycosyltransferases, which are bifunctional C-glycoside arabinosyltransferases and C-glycoside glucosyltransferases. The glycosyltransferases can specifically and efficiently catalyze C-glycoside arabinosylation and glucosylation of dihydrochalcone compounds or 2-hydroxyflavanone compounds, to generate C-glycoside dihydrochalcone or C-glycoside-2-hydroxyflavanone compounds; the C-glycoside-2-hydroxyflavanone compounds are further subjected to a dehydration reaction to form flavone-C-glycoside compounds. The present disclosure also provides an application of the novel UDP-glycosyltransferases to artificially constructed recombinant expression systems to generate C-glycoside dihydrochalcone and flavone-C-glycoside compounds by means of fermentation engineering.

The present disclosure provides recombinant bacterial cells that have been engineered with genetic circuitry which allow the recombinant bacterial cells to sense a patient's internal environment and respond by turning an engineered metabolic pathway on or off. When turned on, the recombinant bacterial cells complete all of the steps in a metabolic pathway to achieve a therapeutic effect in a host subject. These recombinant bacterial cells are designed to drive therapeutic effects throughout the body of a host from a point of origin of the microbiome. Specifically, the present disclosure provides recombinant bacterial cells that comprise a uric acid catabolism enzyme, e.g., a uric acid degrading enzyme, for the treatment of diseases and disorders associated with uric acid, including hyperuricemia and gout, in a subject. The disclosure further provides pharmaceutical compositions and methods of treating disorders associated with uric acid, such as hyperuricemia.

A recombinant vector containing the immunogenic protein of African swine fever virus, a recombinant bacterium and use thereof, and relates to the technical field of gene recombination. The recombinant vector can be used to construct a recombinant Lactobacillus expressing the immunogenic protein of African swine fever virus, and after mixing the Lactobacillus solution that can secrete protein p72 and protein p54, respectively, an oral live bacterial preparation for preventing African swine fever can be prepared. The oral live bacteria preparation prepared by the disclosure can safely, effectively and quickly prevent the infection of African swine fever virus to pigs, and does not contain an immune process.

Described herein are olivetolic acid cyclases (OAC) including non-natural variants capable of forming a 2,4-dihydroxy-6-alkylbenzoic acid from a 3,5,7-trioxoacyl-CoA or a 3,5,7-trioxocarboxylate substrate. In some examples, the non-natural OAC is capable of forming a 2,4-dihydroxy-6-alkylbenzoic acid from a 3,5,7-trioxoacyl-CoA or a 3,5,7-trioxocarboxylate substrate at a greater rate. In some examples, the non-natural OAC has a higher affinity for a 3,5,7-trioxoacyl-CoA or a 3,5,7-trioxocarboxylate substrate, as compared to the wild type OAC. The non-natural OAC can be used with olivetol synthase (OLS) to form the 2,4-dihydroxy-6-alkylbenzoic acid from malonyl-CoA and acyl-CoA through to a 3,5,7-trioxoacyl-CoAintermediate. The non-natural OAC (and OLS) can be expressed in an engineered cell having a pathway to form cannabinoids, which include CBGA, its analogs and derivatives. CBGA can be used for the preparation of cannabigerol (CBG), which can be used in therapeutic compositions.

The present disclosure discloses an Escherichia coli-based genetically-modified recombinant strain, a construction method therefor and use thereof. A mutant gene obtained by subjecting a wild-type deoB gene (ORF sequence is shown in a sequence 3902352-3903575 in GenBank accession No. CP032667.1) and a wild-type rhtA gene promoter sequence PrhtA (shown in a sequence 850520-850871 in GenBank accession No. AP009048.1) of an E. coli K12 strain and a derivative strain thereof (such as MG1655 and W3110) to site-directed mutagenesis, and a recombinant strain obtained therefrom can be used for the production of L-threonine, and compared with an unmutated wild-type strain, the obtained strain can produce L-threonine with a higher concentration and has good strain stability, and also has lower production cost as an L-threonine production strain.

Provided is a transformed microorganism that has a polyhydroxyalkanoate synthase gene and in which expression of an A1386 gene and/or an A2405 gene is reduced. In the transformed microorganism, expression of a minC gene and a minD gene may be enhanced. Also provided is a method of producing a PHA, the method including the step of culturing the transformed microorganism in the presence of a carbon source.

Provided is a method for screening a Corynebacterium constitutive expression vector promoter on the basis of transcriptome sequencing; and further provided are the Corynebacterium constitutive expression vector promoter screened on the basis of transcriptome sequencing, an expression vector comprising the promoter, a recombination strain obtained by transforming a host cell Corynebacterium glutamicum using the expression vector, and applications thereof.

A fusion protein includes heat shock protein 10 and brazzein protein. The fusion protein has an enhanced anti-oxidation activity and skin cell proliferation effect. It can be used as a cosmetic composition for ameliorating skin wrinkles. The cosmetic composition including the fusion protein can be advantageously used in future as a material of a functional cosmetic product.

A recombinant vector of a thermolabile UNG fused protein and an expressing and purifying method are provided. The method comprises cloning a Cod UNG genetic sequence to a pCold-SUMO vector to construct a recombinant vector pCold-SUMO-Cod UNG, transforming to E. coli BL21 (DE3) competent cells, transforming and expressing molecular chaperone plasmids pG-Tf2, and inducing the expression at a low temperature to obtain a soluble SUMO-Cod UNG fused protein.