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Optimization of glutathione production in batch and fed-batch cultures by the wild-type and recombinant strains of the methylotrophic yeast <Emphasis Type="Italic">Hansenula polymorpha</Emphasis>DL-1
Authors:Vira M Ubiyvovk  Vladimir M Ananin  Alexander Y Malyshev  Hyun Ah Kang  Andriy A Sibirny
Institution:(1) Institute of Cell Biology NAS of Ukraine, Drahomanov Street, 14/16, 79005 Lviv, Ukraine;(2) Korea Research Institute of Bioscience and Biotechnology, 305-333 Daejeon, Korea;(3) Department of Life Science, Chung-Ang University, 156-756 Heukseok-dong, Dongjak-gu, Seoul, Korea;(4) University of Rzeszow, Cwiklinskiej 2, 35-601 Rzeszow, Poland
Abstract:

Background  

Tripeptide glutathione (gamma-glutamyl-L-cysteinyl-glycine) is the most abundant non-protein thiol that protects cells from metabolic and oxidative stresses and is widely used as medicine, food additives and in cosmetic industry. The methylotrophic yeast Hansenula polymorpha is regarded as a rich source of glutathione due to the role of this thiol in detoxifications of key intermediates of methanol metabolism. Cellular and extracellular glutathione production of H. polymorpha DL-1 in the wild type and recombinant strains which overexpress genes of glutathione biosynthesis (GSH2) and its precursor cysteine (MET4) was studied.
Keywords:
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