Glyceraldehyde-3-phosphate dehydrogenase mutant and its application in increasing the production of O-succinyl-L-homoserine

By mutation of glyceraldehyde-3-phosphate dehydrogenase and heterologously expressed in E. coli, the problem of insufficient NADPH supply was solved, and the production of O-succinyl-L-homoserine was significantly improved.

CN116042553BActive Publication Date: 2025-08-26ZHEJIANG UNIV OF TECH
2 Cites 0 Cited by

Patent Information

Application Number
CN202211706302.1
Authority / Receiving Office
CN · China
Patent Type
Patents(China)
Current Assignee / Owner
Filing Date
2022-12-29
Publication Date
2025-08-26
Estimated Expiration
2042-12-29

AI Technical Summary

Technical Problem

In the prior art, insufficient supply of NADPH has become a limiting factor that limits the further increase in O-succinyl-L-homoserine production, especially in the fermentation process of E. coli as a production strain.

Method used

Glyceraldehyde-3-phosphate dehydrogenase derived from Flora acetobutyrate was mutated through molecular modification technology to obtain glyceraldehyde-3-phosphate dehydrogenase mutants and expressed heterologously in E. coli to increase the supply of NADPH to increase the synthetic yield of O-succinyl-L-homoserine.

Benefits of technology

The production of O-succinyl-L-homoserine was significantly increased, wild-type gapC increased from 87g/L to 102g/L in recombinant E. coli, mutant gapC increased further to 135g/L in recombinant E. coli, and NADPH supply increased by 50%.

✦ Generated by Eureka AI based on patent content.
Patent Text Reader

Abstract

The present invention discloses a glyceraldehyde 3-phosphate dehydrogenase mutant and its application in increasing the yield of O-succinyl-L-homoserine, wherein the mutant is obtained by single mutation of the arginine at position 233 of the amino acid sequence shown in SEQ ID NO.2. The present invention uses recombinant Escherichia coli producing O-succinyl-L-homoserine as the target strain, introduces exogenous glyceraldehyde 3-phosphate dehydrogenase gapC and its mutant to provide more NADPH supply for the metabolic pathway to increase the yield of OSH. The wild-type gapC provided by the present invention is expressed in recombinant Escherichia coli and can increase the yield of OSH in a 5L fermentor from the original 87g / L to 102g / L, and after the gapC mutant is expressed in recombinant Escherichia coli, the yield of OSH in a 5L fermentor increases to 135g / L, and the supply of NADPH is increased by 50% over the original strain.
Need to check novelty before this filing date? Find Prior Art