한국미생물·생명공학회지 (Microbiology and Biotechnology Letters)
- 제14권6호
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- Pages.447-453
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- 1986
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- 1598-642X(pISSN)
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- 2234-7305(eISSN)
고온, 알칼리성 Bacillus K17이 생성하는 Xylanase의 정제 및 특성
Purification and Characteristics of Xylanases from Produced Thermophilic Alkalophilic Bacillus K17
- Kang, In-Soo (Department of Food and Nutrition, Chinju Technical College) ;
- Sung, Nack-Kie (Department of Food Science and Technology, Gyeong Sang National University) ;
- Chun, Hyo-Kon (Department of Food Science and Technology, Gyeong Sang National University) ;
- Teruhiko Akiba (The Institute of Physical and Chemical Research) ;
- Koki Horikoshi (The Institute of Physical and Chemical Research)
- 발행 : 1986.12.01
초록
고온, 알칼리성 Bacillus K17이 생성하는 extracellular xylanase를 각종 resin으로 정제하여 비흡착 분획에서 xylanase I과 흡착 분획에서 xylanase II를 분리정제하였고, SDS-Polyacrylamide gel electrophoresis에 의하여 분자량을 측정하였던바 xylanase I은 23,000, xylanase II는 47,000으로 추정되었다. Xylanase I 및 II는 최적온도, 최적 pH, 열 안정성, pH 안정성, 기질 친화력에서 차이가 있었으며 Cu
The culture filtrate of thermophilic alkalophilic Bacillus K17 strain contained two types of xylanases were purified by ammonium sulfate fractionation, DEAD-Sephadex A-50 column chromatography, CM-Sephadex C-50 column chromatography and Sephadex G-100 gel filtration. The purified enzymes were found to be homogeneous by sodium dodecyl sulfate and disc polyacrylamide gel electrophoresis. Xylanase I and II were characterized with respect to molecular weight, optimal temperature and pH, thermal and pH stability, and Michaelis constant. Xylanase II was more active and stable, and showed greater substrate affinity and molecular weight than xylanase I. The activities of xylanases I and II were inhibited by Cu