Production of S-lactoylglutathione by glycerol-adapted Saccharomyces cerevisiae and genetically engineered Escherichia coli cells
Tóm tắt
The enzymatic production of S-lactoylglutathione was studied by applying glyoxalase I to glycerol-grown cells of Saccharomyces cerevisiae and Escherichia coli cells dosed with Pseudomonas putida glyoxalase I gene. The glyoxalase I in S. cerevisiae cells was markedly induced when the cells were grown on glycerol. The activity of the enzyme in glycerol-grown cells was more than 20-fold higher compared with that of the glucose-grown cells. By using extracts of glycerol-grown yeast cells, about 5 mmol/1 (2 g/l) of S-lactoylglutathione was produced from 10 mM methylglyoxal and 50 mM glutathione within 1 h. The extracts of E. coli cells carrying a hybrid plasmid pGI423, which contains P. putida glyoxalase I gene, showed approximately 170-fold higher glyoxalase I activity than that of E. coli cells without pGI423. The extracts were used for production of S-lactoylglutathione and, under optimal conditions, about 40 mmol/l (15 g/l) of S-lactoylglutathione was produced from 50 mM methylglyoxal and 100mM glutathione within 1 h.
Tài liệu tham khảo
Davis BD, Mingioli ES (1950) Mutants of Escherichia coli requiring methionine or vitamin B12. J Bacteriol 60:17–28
Gillespie E (1975) Cell-free microtubule assembly: evidence for control by glyoxalase. Fed Proc 34:541
Gillespie E (1979) Effects of S-lactoylglutathione and inhibitors of glyoxalase I on histamine release from human leukocytes. Nature 277:135–136
Gillespie E (1981) The tumor promoting phorbol diester, 12-O-tetradecanoylphorbol-13-acetate (TPA) increases glyoxalase I and decreases glyoxalase II activity in human polymorphonuclear leukocytes. Biochem Biophys Res Commun 98:463–470
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the folin phenol reagent. J Biol Chem 193:265–275
Murata K, Fukuda Y, Watanabe K, Saikusa T, Kimura A (1985) Metabolism of 2-oxoaldehydes in yeast: purification and characterization of NADPH-dependent methylglyoxal reducing enzyme from Saccharomyces cerevisiae. Eur J Biochem 151:631–636
Murata K, Inoue Y, Watanabe K, Fukuda Y, Saikusa T, Shimosaka M, Kimura A (1986a) Metabolism of 2-oxaldehydes in yeast: purification and characterization of glyoxalase II from Saccharomyces cerevisiae. Agric Biol Chem 150:135–142
Murata K, Watanabe K, Inoue Y, Fukuda Y, Shimosaka M, Kimura A (1986b) Complete purification of yeast glyoxalase I and its activation by ferrous ions and polyamines. Agric Biol Chem 50:2381–2383
Murata K, Sato N, Rhee HI, Watanabe K, Kimura A (1987) Purification and characterization of glutathione thiol esterase from Saccharomyces cerevisiae. Agric Biol Chem 51:1901–1907
Penninckx MJ, Jaspers CJ, Legrain MJ (1983) The glutathione-dependent glyoxalase pathway in the yeast Saccharomyces cerevisiae. J Biol Chem 258:6030–6036
Rhee HI, Murata K, Kimura A (1986) Purification and characterization of glyoxalase I from Pseudomonas putida. Biochem Biophys Res Commun 141:993–999
Rhee HI, Murata K, Kimura A (1987) Molecular cloning of the Pseudomonas putida glyoxalase I gene in Escherichia coli. Biochem Biophys Res Commun 147:831–838
Uotila L (1973) Preparation and assay of glutathione thiol esters. Survey of human liver glutathione thiol esterases. Biochemistry 12:3938–3943