Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Production of Selenium Peptide by Autolysis of Saccharomyces cerevisiae

  • Lee Jung-Ok (Department of Biological Engineering, Division of Chemical Science and Biological Engineering, Korea University) ;
  • Kim Young-Ok (Department of Biological Engineering, Division of Chemical Science and Biological Engineering, Korea University) ;
  • Shin Dong-Hoon (Department of Food & Biotechnology, Korea University) ;
  • Shin Jeong-Hyun (Department of Dermatology, College of Medicine, Inha University) ;
  • Kim Eun-Ki (Department of Biological Engineering, Division of Chemical Science and Biological Engineering, Korea University)
  • Published : 2006.07.01
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Abstract

Selenium-containing peptide (selenium peptide) was produced by autolysis of total proteins of Saccharomyces cerevisiae grown with inorganic selenium. Selenium peptide exhibited antioxidant activity as a glutathione peroxidase (GPx) mimic, and its activity was dependent on the hydrolysis methods. The GPx-like activity of the hydrolyzed selenium peptide increased 2.7-folds when digested by protease, but decreased by acid hydrolysis. During the autolysis of the yeast cell, the GPx-like activity and selenium content increased 4.3- and 2.3-folds, respectively, whereas the average molecular weight (MW) of selenium peptide decreased 70%. The GPx-like activity was dependent on the MW of selenium peptide and was the highest (220 U/mg protein) at 9,500 dalton. The maximum GPx-like activity (28,600 U/g cell) was obtained by 48 h of autolysis of the cells, which were precultured with 20 ppm of selenate. Selenium peptide showed little toxicity, compared with highly toxic inorganic selenium. These results show the potential of selenium peptide as a nontoxic antioxidant that can be produced by simple autolysis of yeast cells.

Keywords

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