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RISS 인기검색어
- 검색키워드
- 저자 : 변시명 ( Baek Hie Nahm (검색결과 3 건)
- 무료
- 기관 내 무료
- 유료
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Purification and Characterization of Inulase from Kluyveromyces fragilis
남백희,변시명,Nahm, Baek-Hie,Byun, Si-Myung 생화학분자생물학회 1977 한국생화학회지 Vol.10 No.2
Kluyνeromyces fragilis를 돼지감자 추출액 배지에 배양하여 배지내에 분비된 inulase를 Sepharose 6B겔로 여과한 후 DEAE-Sephadex A-50을 사용하여 효소를 정제 하였다. 이 방법에 의하여 232배 정제하였으며 정제된 효소는 5% polyacrylamide 전기 영동상에서 순수함을 알았다. 순수 분리한 효소를 사용하여 효소의 성질을 조사하였으며 이 효소는 탄수화물을 구성물질로 함유하는 당단백질임을 밝혔다. 효소는 기질에 따라 최적 pH, 최적 온도 및 Km 등이 달랐으나 inulin과 sucrose를 다 분해할 수 있음을 알았다. inulin의 가수분해 양상은 single-chain mechanism 임을 밝혔다. Extracellular inulase which hydrolyzes $\beta$-2:1' linked fructose polymer, inulin, was prepared from Kluyveromyces fragilis in the media containing the Jerusalem artichoke tuber extract. Further purification of the enzyme by Sepharose 6B gel filtration followed by DEAE-Sephadex A-50 ion exchange chromatography showed a single protein band on 5% polyacrylamide gel electrophoresis with 232-fold purification. Using the purified enzyme some kinetic parameters of inulase were studied with comparison of invertase activity on sucrose. The enzyme was found to be a glycoprotein and had both inulase and invertase activities, although the general properties varied against substrates in terms of pH, Km, and temperature. The mode of hydrolytic action on inulin by the purified enzyme preparation appeared to be single chain mechanism.
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Kluyveromyces fragilis 의 Inulase 분리 정제
남백희,변시명 ( Baek Hie Nahm,Si Myung Byun ) 생화학분자생물학회 1977 BMB Reports Vol.10 No.2
Extracellular inulase which hydrolyzes β-2:1` linked fructose polymer, inulin, was prepared from Kluyveromyces fragilis in the media containing the Jerusalem artichoke tuber extract. Further purification of the enzyme by Sepharose GB gel filtration followed by DEAE-Sephadex A-50 ion exchange chromatography showed a single protein band on 5% polyacrylamide gel electrophoresis with 232-fold purification. Using the purified enzyme some kinetic parameters of inulase were studied with comparison of invertase activity on sucrose. The enzyme was found to be a glycoprotein and had both inulase and invertase activities, although the general properties varied against substrates in terms of pH, Km, and temperature. The mode of hydrolytic action on inulin by the purified enzyme preparation appeared to be single chain mechanism.
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