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Journal of Solid Phase Biochemistry

, Volume 3, Issue 4, pp 247–261 | Cite as

Production ofl-aspartic acid byE. coli aspartase immobilized on phenol-formaldehyde resin

  • Yasuharu Yokote
  • Shohachi Maeda
  • Hisao Yabushita
  • Sadao Noguchi
  • Kazuo Kimura
  • Hirotoshi Samejima
Article

Abstract

Aspartase was extracted from E. coli cells by autolysis in the presence of the substrate. The enzyme could be conveniently immobilized to a weakly basic anion exchange resin Duolite A7 by adsorption. Enzymatic properties of the immobilized aspartase were found to be fit for industrial purposes. Consequently,l-aspartic acid has been industrially produced by this immobilized-enzyme process since 1974.

Keywords

Immobilize Enzyme Fumaric Acid Basic Anion Exchange Resin Activity Protein Activity Aspartase Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Humana Press Inc. 1978

Authors and Affiliations

  • Yasuharu Yokote
    • 1
  • Shohachi Maeda
    • 1
    • 2
  • Hisao Yabushita
    • 1
  • Sadao Noguchi
    • 1
  • Kazuo Kimura
    • 1
  • Hirotoshi Samejima
    • 1
  1. 1.Tokyo Research Laboratory of Kyawa Hakko Kogyo Co., Ltd.TokyoJapan
  2. 2.Technical Research Laboratory of Hofu Plant of Kyowa Hakko Kogyo Co., Ltd.YamaguchiJapan

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