NAD < + > dependent formate dehydrogenase mutant

• Main Authors: NI YEWEN, WU QIANQIAN, LIU ZUOYANG, GUAN JIAWEI
• Format: Patent
• Language: Chinese; English
• Published: 31.05.2024
• Subjects: BEER; BIOCHEMISTRY; CHEMISTRY; COMPOSITIONS THEREOF; CULTURE MEDIA; ENZYMOLOGY; FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIREDCHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERSFROM A RACEMIC MIXTURE; METALLURGY; MICROBIOLOGY; MICROORGANISMS OR ENZYMES; MUTATION OR GENETIC ENGINEERING; PROCESSES USING MICROORGANISMS; PROPAGATING, PRESERVING OR MAINTAINING MICROORGANISMS; SPIRITS; VINEGAR; WINE

The invention discloses an NAD < + > dependent formate dehydrogenase mutant. The thermal stability of the mutant designed by the invention is superior to that of a wild type. The thermal stability of a mutant formed by any combination of P106A, S132A, R136H, I280L, T340S, F397Y and K398E is better, and the thermal stability of the mutant formed by any combination of P106A, S132A, R136H, I280L, T340S, F397Y and K398E is better, so that the thermal stability of the mutant is better. The residual enzyme activity of the mutant obtained by combined mutation after being incubated at 60 DEG C for 90 minutes can reach 296.7% of that of a wild type. Therefore, an NAD < + >-NADH reaction system in which the formate dehydrogenase mutant participates can react at a relatively high temperature, the catalytic efficiency of the reaction system is obviously improved, and the production efficiency of NADH is improved. 本发明公开了一种NAD+依赖型甲酸脱氢酶突变体，本发明设计的突变体的热稳定性均优于野生型。排除"在没有P106A或/和T340S突变，R136H和I280L两个突变位点同时存在"的情况，P106A、S132A、R136