Overproduction of glutathione and its derivatives by genetically engineered microbial cells

Abstract

In order to improve the biotechnological potentials of Escherichia coli cells to produce glutathione, S- d-lactoylglutathione and other γ-glutamyl compounds, the genes for enzymes [γ-L-glutamyl-L-cysteine synthetase (GSH A) in E. coli B, glutathione synthetase (GSH B) in E. coli B, glyoxalase I (GLO I) in Pseudomonas putida] were cloned and amplified in E. coli. E. coli B cells transformed with both GSH A and GSH B genes exhibited a high activity in the synthesis of glutathione and other γ-glutamyl compounds in bioreactor systems containing immobilized cells. E. coli C600 cells transformed with GLO I gene of P. putida showed a high GLO I activity and were used for the preparation of S- d-lactoylglutathione and other glutathione thiol esters.