Structural Conversion from Non-native to Native form of Recombinant Human Epidermal Growth Factor by Brevibacillus choshinensis.

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  • MIYAUCHI Akira
    R & D Department, Higeta Shoyu Co., Ltd. Department of Biotechnology, Graduate School of Science and Technology, Chiba University
  • OZAWA Makoto
    R & D Department, Higeta Shoyu Co., Ltd.
  • MIZUKAMI Makoto
    R & D Department, Higeta Shoyu Co., Ltd.
  • YASHIRO Kouji
    R & D Department, Higeta Shoyu Co., Ltd.
  • EBISU Shogo
    R & D Department, Higeta Shoyu Co., Ltd.
  • TOJO Takashi
    R & D Department, Higeta Shoyu Co., Ltd.
  • FUJII Takaaki
    Department of Biotechnology, Graduate School of Science and Technology, Chiba University
  • TAKAGI Hiroaki
    R & D Department, Higeta Shoyu Co., Ltd. Department of Biotechnology, Graduate School of Science and Technology, Chiba University

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  • Structural Conversion from Non-native to Native form of Recombinant Human Epidermal Growth Factor by<i>Brevibacillus choshinensis</i>

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Abstract

  Brevibacillus choshinensis (Bacillus brevis) HPD31 is a very efficient producer of recombinant human epidermal growth factor (EGF). The produced EGF is secreted into the medium with high efficiency. However part of the EGF that accumulates in the medium, exists as multimeric forms which are biologically inactive. We found the bacterium has the activity to structurally convert multimeric forms to the monomeric, native ones. Optimal temperature and pH for the conversion were 40°C and pH 9, respectively. The reaction was promoted in the presence of reduced glutathione or cysteine. But the cells which had been sonicated or exposed to moderate heat treatment completely lost the activity. Thus, it was presumed that the activity might be due to the enzyme(s) that catalyze the protein disulfide exchanging reaction, and that they resides on the surface of viable cells.<br>

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