Microbiology and Biotechnology Letters (한국미생물·생명공학회지)

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Immobilization and Characterization of Rifamycin B Oxidase in Cellulose Acetate Beads

셀룰로오스 아세테이트에 고정화된 리파마이신 B 산화효소의 특성

  • Chung, Bong-Hyun (Department of Chemical Engineering and Genetic Engineering Research Center Korea Advanced Institute of Science and Technology) ;
  • Chang, Ho-Nam (Department of Chemical Engineering and Genetic Engineering Research Center Korea Advanced Institute of Science and Technology) ;
  • Han, Moon-Hi (Department of Chemical Engineering and Genetic Engineering Research Center Korea Advanced Institute of Science and Technology)
  • Published : 1985.06.01
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Abstract

Rifamycin B oxidase converts rifamycin B to rifamycin S using oxygen as cosubstrate. Humnicola spp. (ATCC 20620) was treated with acetone and the cell powder was immobilized with cellulose acetate. The properties of the immobilized enzyme was examined. The optimum pHs of the immobilized and the free enzymes were 7.2. The optimum temperature of the immobilized enzyme was at 50-55$^{\circ}C$, which was 5$^{\circ}C$ higher than that of the free enzyme. The activities of the immobilized enzyme appeared less sensistive with respect to the changes of temperature and pH as compared to those of the free enzyme. Twenty percent of the enzyme activity was recovered when the enzyme was immobilized in 3mm beads. The storage stability was good below 4$0^{\circ}C$, but the activity decreased very rapidly above 5$0^{\circ}C$. The physical strength of the beads was good and was suitable as packing material in a three-phase enzyme reactor.

리파마이신 B 산화효소의 활성을 갖고 있는 Humicola spp. (ATCC 20620)를 아세톤 처리 한 후 cellulose acetate로 고정화하여 그 특성을 조사하였다. 고정화 효소에 있어서 pH는 7.2온도는 50-55%에서 최대 활성을 보였으며, 비고정화 효소에 비하여 pH와 온도변화에 덜 민감하였다. 외경 3mm bead size에서 20%의 활성회수율을 보였으며, storage stability는 4$0^{\circ}C$ 이하에서는 아주 좋았으며 5$0^{\circ}C$ 이상에서는 급격히 활성이 감소하였다. 고정화 담체로서 cellulose acetate는 물리적으로 견고하여 삼상반응기의 packing material로써 적당하였다.

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