11 results about "Phosphoglucomutase" patented technology

The invention provides an application of inositol monophosphate in an enzyme catalysis reaction system for preparing inositol. The invention also provides a preparation method of the inositol, the starch is used as a substrate, glucan phosphorylase, glucose phosphate mutase, inositol-3-phosphate synthase and inositol monophosphate are added as enzyme catalysts to catalyze the substrate to generate the inositol, the inositol monophosphate is derived from Archaeoglobus fulgidus, the amino acid sequence is shown as SEQ ID NO: 12, or the amino acid sequence is shown as SEQ ID NO: 1, or the amino acid sequence is shown as SEQ ID NO: 2, or the amino acid sequence is shown as SEQ ID NO: 3, or the amino acid sequence is shown as SEQ ID NO: 4, or the amino acid sequence is shown as SEQ ID NO: 5, or the amino acid sequence is shown as SEQ ID NO: 6. The inositol monophosphate is derived from Thermococcus kodakarensis, and the amino acid sequence of the inositol monophosphate is as shown in SEQ ID NO: 13; or the inositol monophosphate is derived from Pseudothermotoga lettinae, and the amino acid sequence of the inositol monophosphate is as shown in SEQ ID NO: 14. Inositol-3-phosphate synthetase and inositol monophosphate with good performance are screened, high-concentration starch is efficiently catalyzed to be converted into inositol by a one-pot method in a whole-cell feeding mode, and NAD < + > and other coenzymes do not need to be used. Under a 60L reaction system, 200g / L of corn starch is catalyzed, the unit yield of the prepared inositol reaches 161g / L, and the method has a good industrial application prospect.

The inventive technology described herein includes systems, methods, and compositions for the upregulation of Uridine diphosphate glucose (UDPG) recycling in a yeast cell, by expressing a heterologous nucleotide sequence, operably linked to a promoter, encoding a phosphoglucomutase enzyme which catalyzes the conversion from glucose-6-phosphate to glucose- 1 -phosphate, and a UDP-glucose pyrophosphorylase enzyme which catalyzes the formation of UDPG from glucose 1 -phosphate and UTP. The increased levels of UDPG substrate produced by the yeast cell may be used as a substrate for a co-expressed UDP -glycosyltransferases enzyme capable of generating cannabinoid glycoside compounds.

The present application relates to the technical field of biotechnology, and particularly relates to a tagatose-6-phosphate phosphatase mutant and a method for synthesizing tagatose from scratch. The method provided by the present application is a one-pot method for biosynthesizing D-tagatose by using starch or dextrin as a substrate, adopting a multi-enzyme cascade reaction system composed of a tagatose-6-phosphate phosphatase mutant, a glycogen-debranching enzyme, an alpha-glucan phosphorylase, a phosphoglucomutase, a glucose-6-phosphate isomerase, a D-tagatose-6-phosphate-3-epimerase and a 4-alpha-glucan transferase. The method can prepare tagatose from ordinary and inexpensive starting materials (starch or dextrin) at a high yield, improves the overall conversion rate of the system and the final yield of tagatose, provides a new technical approach for realizing low-cost and green production of tagatose, and has the advantages of high yield, low cost and being more suitable for industrial production.

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.

The application discloses a phosphoglucomutase, a mutant and application of the phosphoglucomutase and the mutant in improving yield of exocellular polysaccharide of lactic acid bacteria, and relates to the technical field of microbial engineering. The amino acid sequence of the phosphoglucomutase is shown as SEQ ID NO. 1. After the phosphoglucomutase is transferred into a host cell, the yield of exocellular polysaccharide of the lactic acid bacteria can be improved. Further, the amino acid at position 526 of the phosphoglucomutase from tetragenococcus halophilus is mutated, and the phosphoglucomutase mutant with T526I mutation can further improve the yield of exocellular polysaccharide of the lactic acid bacteria.

This invention provides a hydrogen production reaction system using formaldehyde and water as co-substrates, comprising a buffer solution, maltodextrin, formaldehyde, magnesium chloride, manganese chloride, NAD, benzyl viologen, sodium phosphate, α-glucan phosphorylase, phosphogluconomutase, glucose-6-phosphate dehydrogenase, phosphogluconate dehydrogenase, phosphogluconolactonease, flavoxase, hydrogenase, 6-phosphate hexulose synthase, phosphogluconose isomerase, and phosphogluconose isomerase. This invention also provides a corresponding hydrogen production method. This invention utilizes formaldehyde and water to generate hydrogen, avoiding excessive dependence on agricultural resources; simultaneously, by replacing traditional carbohydrates with high-energy formaldehyde as the substrate, it lowers the energy barrier of the co-substrate water and simplifies the process of carbohydrate miniaturization and hydrogen production; furthermore, it has the advantages of being less demanding in terms of water quality conditions and having low cost.

The present disclosure relates to an engineered organism comprising at least one sucrose phosphorylase encoding gene; at least one sucrose permease encoding gene; and at least one phosphoglucomutase encoding gene, such that said engineered organism utilizes sucrose, wherein said engineered organism has ≥ 90% homology to Cupriavidus genus The present disclosure further relates to a method for carrying out fermentation using the engineered organism in the presence of sucrose, such that sucrose is utilized.

The invention belongs to the technical field of genetic engineering, and particularly relates to a genetically engineered bacterium for efficiently synthesizing betacyanin as well as a construction method and application of the genetically engineered bacterium. According to the invention, a gene editing technology is used for jointly enhancing the expression levels of phosphoglucomutase pgm and UDP-glucose pyrophosphorylase galU on a BL21 (DE3) genome, the supply level of uridine diphosphate glucose which is a precursor substance for synthesizing betacyanin can be effectively improved, and a genetically engineered bacterium is constructed by combining a double-plasmid multienzyme expression system and overexpressing hpaBC, dodA, CYP76AD1 and 5GT. The engineering bacterium realizes whole-cell catalytic synthesis of betacyanin by taking tyrosine and glucose as direct substrates for the first time through collaborative optimization of genome editing and a plasmid expression system, and the product yield and the process economy are remarkably improved.

The invention belongs to the field of molecular biology, and particularly relates to a construction method and application of phosphorylation mutation sites of phosphoglucomutase. The mutation site is obtained by mutating threonine at the 144th site of escherichia coli wild-type phosphoglucomutase into aspartic acid, the sensitivity of an escherichia coli mutant strain with the mutation site to nalidixic acid, mitomycin C and tetracycline is remarkably improved, and the mutation site can be used for improving the sensitivity of bacteria to drugs.

The invention relates to a property-changed phosphoglucomutase mutant and application thereof, and belongs to the technical field of enzyme engineering. According to the invention, the phosphoglucomutase is mutated at different sites, the property of the obtained phosphoglucomutase mutant is changed, especially the thermal stability of the phosphoglucomutase mutant is obviously improved, the residual enzyme activity of the phosphoglucomutase mutant at 30 DEG C is also greatly improved at 65 DEG C, and the residual enzyme activity of the phosphoglucomutase mutant at 65 DEG C is also greatly improved. Therefore, the phosphoglucomutase mutant disclosed by the invention can still keep good enzyme activity in a biological process needing to be carried out at high temperature, and has wide application value in industrial application.

The present application relates to the field of biological catalysis engineering, and particularly relates to a method for synthesizing amylose by three-enzyme cascade catalysis of glucose. The method comprises: phosphorylating the substrate glucose into an intermediate G-6-P in the presence of polyphosphoric acid by a heat-resistant polyphosphate glucose kinase; shifting G-6-P into G-1-P by a heat-resistant phosphoglucomutase, and adding the intermediate G-1-P to the non-reducing end of oligosaccharide to synthesize amylose by a heat-resistant alpha-dextran phosphorylase. The present application optimizes the reaction conditions of the reaction system for synthesizing amylose by glucose, and explores the most suitable metal ion type and concentration, pH, and buffer type. In the reaction process of the three-enzyme cascade catalysis of glucose for preparing amylose after optimization, the conversion rate is 71.93%, the yield reaches 3.5 g / L, and the space-time yield is 2.33 g / L / h.