Studies on Microbial Penicillin Amidase (II) Characteristics and the Reactor Performance of Whole Cell Immobilized Penicillin Amidase of Escherichia coli

미생물 페니실린 아미다제에 관한 연구 (II) E. coli의 균체 고정화 페니실린 아미다제의 특성 및 반응조에 관한 연구

  • Seong, Baik-Lin (Biotechnology Research Department, Korea Institute of Science and Technology) ;
  • Kim, Bong-Hee (Biotechnology Research Department, Korea Institute of Science and Technology) ;
  • Mheen, Tae-Iek (Biotechnology Research Department, Korea Institute of Science and Technology) ;
  • Moon H. Han (Biotechnology Research Department, Korea Institute of Science and Technology)
  • Published : 1981.03.01

Abstract

Whole cell penicillin amidase of Escherichia coli was immobilized by entrapment in gelatin followed by extrusion and crosslinking with glutaraldehyde. The immobilized engyme preparation demonstrated the recovery yield of activity up to 70% and good stability during storage and operation. The half life of activity decay during the operation was estimated to be about 50 days. The optimum pH and temperature for both of immobilized and soluble enzyme are 8.5 and 5$0^{\circ}C$, respectively. No significant change was demonstrated in the effect of pH and temperature, but the increase in heat stability at high temperature was observed in the case of the immobilized enzyme. It was found that the plug flow reactor could be operated favorably since the pH drop along the column path due to tile reaction product was minimized by employing substrate solution with moderate buffer strength. The optimal condition of reactor operation was discussed with regard to the effect of substrate concentration and the residence time on the conversion efficiency and productivity.

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