한국미생물·생명공학회지 (Microbiology and Biotechnology Letters)
- 제18권4호
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- Pages.360-367
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- 1990
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- 1598-642X(pISSN)
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- 2234-7305(eISSN)
Arthrobacter sp.가 생산하는 Rutinosidase의 정제 및 특성
Purification and Some Properties of Rutinosidase from Arthrobacter sp.
초록
토양으로부터 rutin을 유일한 탄소원으로 생육하는 세균을 분리하여 그 중 rutin 가수분해활성이 높은 MT-57균을 Arthrobacter sp.로 동정하였다. Arthrobacter sp.MT-57에서 수 종류의 rutin 가수분해효소가 확인되었으며 이들 중 rutinosidase를 전기영동상 단일한 효소 단백질까지 정제하였다. Rutinosidase으 분자량은 SDS page와 gel filtration으로 부터 42,000의 단량체로 추정 되었다. 효소반응의 최적 pH와 온도는 pH 7.5와
The several glycoside hydrolysing enzymes related to rutin degradation are found to be rhamnosidase, glucosidase and rutinosidase. Rutinosidase was purified to electrophoretic homogeneity from cell extracts of rutin-degrading strain, MT-57, which was identified as a Arthrobacter sp. Its molecular weight was estimated to be 42, 000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 40, 000 by gel filtration. The optimum pH for enzyme was found to be 7.5, and relatively stable in alkaline solution. The optimum temperature for enzyme was