6results about How to "High substrate conversion rate" patented technology

The application belongs to the technical field of 2,5-furan dicarboxylic acid (FDCA) biosynthesis, and particularly relates to an engineered Pseudomonas and application and a method thereof in 2,5-furan dicarboxylic acid biosynthesis. The engineered Pseudomonas takes MB04S-HMF1 as a starting strain, and 7 copies of a glycerolaldehyde-3-phosphate dehydrogenase gene expression cassette and an aldehyde dehydrogenase gene expression cassette are inserted into a 16s rDNA site of a genome of the starting strain, the glycerolaldehyde-3-phosphate dehydrogenase gene expression cassette comprises P MP00 a promoter, a gapA gene and a gapB gene, and the aldehyde dehydrogenase gene expression cassette comprises P MP00 a promoter and an aldehyde dehydrogenase gene. The engineered strain has good growth performance, extremely high substrate conversion rate and space-time yield, completely eliminates byproduct accumulation, has excellent operation stability and multi-batch recycling ability in continuous multiple recycling, and has extremely high genetic and phenotypic stability.

This application relates to the fields of genetic engineering and enzyme engineering, specifically to an ornithine decarboxylase mutant, gene, recombinant plasmid, recombinant strain, and its applications. The ornithine decarboxylase mutant is obtained by mutating the wild-type ornithine decarboxylase with the amino acid sequence shown in SEQ ID NO.1, and the mutation sites of the ornithine decarboxylase mutant include any one or more of Y104F, A264V, Q263E, R157K, S325C, and V265A. By performing single-point or multi-site combination mutations on the wild-type ornithine decarboxylase, a high-activity ornithine decarboxylase mutant is obtained, thereby significantly improving the substrate conversion rate of the ornithine decarboxylation reaction and the synthesis efficiency of butanediamine. This successfully overcomes the rate-limiting bottleneck of the ornithine decarboxylation reaction in the synthetic pathway from glucose to ornithine and then to butanediamine, significantly optimizing the overall efficiency of this metabolic pathway.

The invention relates to a method for preparing (R)-salbutamol. Specifically, L-threonine and a compound 1 are taken as raw materials, a compound 2 is formed under the catalysis of L-threonine transaldolase, the compound 2 is formed into a compound 3 under the catalysis of decarboxylase, on the basis, the compound 3 is taken as a substrate, and the (R)-salbutamol is further synthesized. And the method has the characteristics of low cost of raw materials and auxiliary materials, short process steps, simplicity and convenience in operation, mild reaction conditions and environmental friendliness.

This invention is a divisional application for "Ornithine Decarboxylase Mutant, Gene, Recombinant Plasmid, Recombinant Strains and Applications," relating to the fields of genetic engineering and enzyme engineering technology, specifically involving an ornithine decarboxylase mutant, gene, recombinant plasmid, recombinant strain, and applications. The ornithine decarboxylase mutant is obtained by mutating the wild-type ornithine decarboxylase with the amino acid sequence shown in SEQ ID NO.1, and the mutation site of the ornithine decarboxylase mutant is Y104F. By performing single-point or multi-site combination mutations on the wild-type ornithine decarboxylase, a high-activity ornithine decarboxylase mutant is obtained, thereby significantly improving the substrate conversion rate of the ornithine decarboxylation reaction and the synthesis efficiency of butanediamine. This successfully overcomes the rate-limiting bottleneck of the ornithine decarboxylation reaction in the synthetic pathway from glucose to ornithine and then to butanediamine, significantly optimizing the overall efficiency of this metabolic pathway.

A novel 2-deoxyribose-5-phosphoaldolase was identified and isolated from Rhodococcus SD3. Rr DeoC), functional studies have shown that this enzyme can catalyze the aldol condensation reaction between acetaldehyde and chloroacetaldehyde, and is used in the synthesis of key intermediates for statin drugs (DeoC). 3R , 5S )-6-chloro-2,4,6-trideoxypyranose. However, wild-type Rr DeoC still suffers from limited catalytic efficiency in the conversion of the non-natural substrate chloroacetaldehyde. To address this issue, this invention combines rational design and virtual screening strategies to improve catalytic efficiency. Rr The DeoC enzyme molecule underwent rational modification. The results showed that... Rr The DeoC mutant S43A achieved a chloroacetaldehyde conversion rate of 69.4% after 1 h of aldol condensation, which was 24.7% higher than that of the wild type. After optimization, the conversion rate of chloroacetaldehyde was further improved to 79.8% after 12 h of aldol condensation.

This invention provides a strain derived from Clostridium difficile (Clostridium difficile) Clostridioides difficile This invention relates to mutants of glutamate dehydrogenase and their applications. The mutants are single-site, two-site, or multi-site mutants of glutamate dehydrogenase. This invention effectively solves the problems of inactivity or low activity of glutamate dehydrogenase in the biocatalytic transformation of 2-carbonyl-4-(hydroxymethylphosphono)butyric acid as a substrate, and provides a continuous chemical method for the synthesis of 2-carbonyl-4-(hydroxymethylphosphono)butyric acid using a microchannel reactor throughout the entire process.