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KMID : 0545119910010030157
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Journal of Microbiology and Biotechnology
1991 Volume.1 No. 3 p.157 ~ p.162
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Amplification of Glutathione Production in E. coli Cells Using Recombinant DNA Techniques
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Nam, Yong Suk
Park, Young In/Lee, Se-Yong
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Abstract
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Conditions for glutathione production in E. coli cells which possess pGH501 (2 gshI+gshII) were studied. In terms of ATP supply for the glutathione synthesis, two different systems have been constructed and compared. When the acetate kinase reaction of E. coli was used for ATP generation, 20mM of L-cysteine was completely converted to glutathione by toluene-treated E. coli cells (100㎎/㎖) harboring pGH501 within 2h at 37℃. However, considering the economical aspects, the glycolytic pathway of yeast was chosen as a better system for ATP generation. The optimal concentrations of reactants for glutathione production were determined to be as follows; 80mM L-glutamate, 20mM L-cysteine, 20mM glycine, 20mM MgCl_2, 50 mM potassium phosphate buffer (pH 7.5), 400 mM glucose, polyoxyethylene stearylamine (5 ㎕/㎖), toluene-treated E. coil HB101/pGH501 (100㎎/㎖), and dried yeast cells (400㎎/㎖). The conversion ratio of L-cysteine to glutathione was 80% (about 5㎎/㎖) under optimal condition within 6 h at 37℃.
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