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

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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.

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Correspondence to Yasuharu Yokote or Shohachi Maeda or Hisao Yabushita or Sadao Noguchi or Kazuo Kimura or Hirotoshi Samejima.

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Yokote, Y., Maeda, S., Yabushita, H. et al. Production ofl-aspartic acid byE. coli aspartase immobilized on phenol-formaldehyde resin. Journal of Solid Phase Biochemistry 3, 247–261 (1978). https://doi.org/10.1007/BF02991851

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  • Immobilize Enzyme
  • Fumaric Acid
  • Basic Anion Exchange Resin
  • Activity Protein Activity
  • Aspartase Activity