12 results about "Mutase" patented technology

The invention relates to the technical field of preparation of L-tyrosine, and discloses a method for enhancing generation of L-tyrosine in nicotiana benthamiana and application. In order to relieve product negative feedback inhibition of a key enzyme in a production path of L-tyrosine in tobacco and to improve the yield of L-tyrosine in tobacco, DAHPS enzyme derived from microorganisms is subjected to L175Q site mutation and then is connected with a signal peptide AtRs1A; shikimic acid mutase / prebenzoate dehydrogenase TyrAfbr and tyrosine aminotransferase TyrB which are derived from microorganisms are introduced into the tobacco chassis after being connected with the signal peptide Rs1A, the expression has orthogonality, and transient expression is performed in the Bensi tobacco plant chassis by utilizing agrobacterium infection, so that the synthesis capability of L-tyrosine in tobacco chassis cells can be improved; a large amount of L-tyrosine can be directly generated in the tobacco chassis plastid.

The application provides a myo-inositol-3-phosphate synthase mutant, which is obtained by mutating a myo-inositol-3-phosphate synthase with an amino acid sequence as shown in SEQ ID NO: 4 at positions 55, 57 and 273 respectively. The application also provides a preparation method of myo-inositol. The inventors have screened a wild-type myo-inositol-3-phosphate synthase and a myo-inositol monophosphatase with good performance, which can be used in cooperation with a glucan phosphorylase and a glucose phosphate mutase to catalyze starch to generate myo-inositol more efficiently. The myo-inositol-3-phosphate synthase mutant is applied to in-vitro non-fermentation biosynthesis of myo-inositol, combined with myo-inositol monophosphatases E1 and E5, and in a way of feeding whole cells, so that starch can be converted into myo-inositol in a one-pot method, without using NAD + coenzymes, and has a good industrial application prospect.

This invention discloses a recombinant glucuronide C5 epimerase mutant, expression vector, recombinant expression engineered bacteria, and their culture and induction methods, belonging to the field of biotechnology. The recombinant enzyme sequence is formed by fusing a truncated (N29–N617) mutation (V173R–V197K–A239V–N269E) with an N-terminal maltose-binding protein (MBP) tag to a human glucuronide C5 epimerase (C5-epi). The recombinant glucuronide C5 epimerase mutant exhibits higher activity, 2.1 times that of the recombinant wild-type, and greater stability, retaining 72.5% of its activity after 5 days at room temperature. Furthermore, the soluble expression level of this recombinant mutant glucuronide C5 epimerase is increased by 4-fold.

The invention relates to the technical field of biological catalysis, and provides a method for catalytic synthesis of trehalose-6-phosphoric acid, key parameters in a multi-enzyme cascade catalytic reaction system for catalytic synthesis of trehalose-6-phosphoric acid are adjusted, and in the catalytic system, the enzyme activity concentration of maltose phosphorylase is 80-120U / mL, the enzyme activity concentration of maltose phosphorylase is 20-30U / mL, and the enzyme activity concentration of maltose phosphorylase is 20-30U / mL. The enzyme activity concentration of the beta-glucophosphate mutase is 15-35 U / mL, the enzyme activity concentration of the trehalose-6-phosphate phosphorylase is 3-15 U / mL, and the yield of the trehalose-6-phosphate can be remarkably improved by adjusting a corresponding production process, so that an enzyme dosage combination with higher universality and high efficiency is obtained, and the method is suitable for industrial production. The conversion rate from the substrate to the target product trehalose-6-phosphoric acid can be up to 96%, the operation is simple and convenient, the cost is low, and the efficient and low-cost industrial production of the trehalose-6-phosphoric acid is realized.

This invention discloses a glucose phosphate mutase gene Rk PGM Its nucleotide sequence is shown in SEQ ID NO:1, and the amino acid sequence encoded by this gene is shown in SEQ ID NO:2; this gene was isolated from *Rhodotorula rubrum* (…). Rhodosporidium kratochvilovae YM25235 was used to ligate the gene to a vector and transfected into Rhodotorula rubrum cells. Experimental results showed that overexpression of Rk... PGM The gene will increase the level of extracellular polysaccharide synthesis in this strain; this invention modifies microorganisms through genetic engineering to improve their ability to secrete extracellular polysaccharides, providing a theoretical basis for increasing the yield of extracellular polysaccharides in Rhodotorula rubrum.

The invention relates to the technical field of microorganisms, and particularly discloses application of phosphomannose mutase mutated microorganisms in fermentation production of L-threonine. The research finds that after the phosphomannose mutase of the microorganism is mutated, the yield of threonine can be increased, and then the application of the microorganism with the mutated phosphomannose mutase in fermentation production of L-threonine is provided. The mutation of the phosphomannose mutase means that glutamic acid is mutated into lysine at the 34th site in the protein sequence of the phosphomannose mutase. The invention provides a novel method for fermentation production of threonine.

The invention discloses a genetically engineered bacterium for producing monensin and application of the genetically engineered bacterium, and belongs to the technical field of metabolic engineering. The invention provides a recombinant cinnamon streptomyces capable of increasing the yield of monensin, the recombinant cinnamon streptomyces simultaneously overexpresses phosphofructokinase (pfk), citrate synthase (cs), methylmalonyl coenzyme A isomerase (mutB) and isobutyryl coenzyme A mutase (icm), and the result shows that the recombinant cinnamon streptomyces overexpresses acetyl coenzyme A synthesis and energy supply of the monensin. According to the method, synthesis precursors (methylmalonyl CoA and ethylmalonyl CoA) are increased, the yield of monensin can be increased without increasing the supply of the precursors, the yield can reach 20.4 g / L, the production cost is effectively reduced, and the production benefit is improved.

An aspect provides a vaccine composition for preventing tuberculosis comprising chorismate mutase. The vaccine composition alone may induce immunity specific to Mycobacterium tuberculosis, and when provided together with an immune adjuvant, the vaccine composition may induce immunity specific to tuberculosis more effectively. Furthermore, when an existing vaccine for tuberculosis is used as a prime and the vaccine composition according to an aspect including chorismite mutase is provided as a booster, the immunity specific to tuberculosis may be induced significantly more effectively.

The invention discloses an N-acetylglucosamine transferase mutant and application thereof in production of L-tryptophan, and belongs to the technical field of genetic engineering. In order to solve the problems of yield limitation and the like caused by excessive consumption of phosphoenolpyruvic acid in the production of L-tryptophan, the invention weakens a phosphoprotein coding gene crr on escherichia coli; meanwhile, a uridine diphosphate galactose pyranose mutase gene glf and a glucokinase gene glk of the pseudomonas mobilis and an endogenous galactose H (+) transporter enzyme gene galP of escherichia coli are integrated at a pflB site, and a genetically engineered bacterium is obtained; mutagenesis is carried out on the basis to obtain a mutant strain with improved L-tryptophan yield; and the N-acetylglucosamine transferase mutants nagC and nagE are obtained by virtue of sequencing. Fermentation proves that overexpression of the mutant nagC or nagE or simultaneous overexpression of the mutants nagC and nagE in the genetically engineered bacteria can improve the yield of L-tryptophan.

The application discloses a kind of recombinant escherichia coli and its construction method and application, the recombinant escherichia coli can be used for the production of L-phenylalanine.The application utilizes multiple rounds of mutagenesis screening to have high resistance to L-phenylalanine structural analogues, and has tyrosine auxotrophic mutant strain, and is regulated in the form of temperature-sensitive recombinant plasmid to code 3-deoxy-7-phosphoheptanoate synthase and branch acid mutase gene expression in L-phenylalanine synthesis pathway.The recombinant escherichia coli constructed in the application, in 5L fermenter, according to the cell growth stage adopts different temperature control and feeding mode, fermentation time is 56 h, under the condition that L-phenylalanine production is 62 g / L, sugar acid conversion rate is 25.2%, has the prospect and value of industrialization application.

The present disclosure is directed to compositions and methods for the treatment of Metabolic Liver Disorders. The compositions and methods can comprise an adeno-associated virus (AAV) piggyBac polynucleotide comprising a transgene. The transgene may comprise ornithine transcarbamylase (OTC) or methylmalonyl-CoA mutase (MUT1).

The present invention provides, among other things, methods and compositions for treating methylmalonic academia (MMA) based on mRNA therapy. The compositions used in treatment of MMA comprise an mRNA comprising a methymalonyl-CoA mutase (MUT) coding sequence and are administered at an effective dose and an administration interval such that at least one symptom or feature of MMA is reduced in intensity, severity, or frequency or has a delayed onset. mRNAs with optimized MUT coding sequences are provided that can be administered without the need for modifying the nucleotides of the mRNA to achieve sustained in vivo function.