한국미생물·생명공학회지 (Microbiology and Biotechnology Letters)
- 제13권2호
- /
- Pages.115-118
- /
- 1985
- /
- 1598-642X(pISSN)
- /
- 2234-7305(eISSN)
셀룰로오스 아세테이트에 고정화된 리파마이신 B 산화효소의 특성
Immobilization and Characterization of Rifamycin B Oxidase in Cellulose Acetate Beads
- 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)
- 발행 : 1985.06.01
초록
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
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
키워드