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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국식품영양과학회 Journal of Food Science and Nutrition Journal of Food Science and Nutrition Vol.2 No.3
- 발행연도
- 1997.9
- 수록면
- 250 - 254 (5page)
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초록· 키워드
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The internal invertase of Rhodosporidium toruloides mating type a cells was purified to a single band on SDS-PAGE from cell-free extract by acid precipitation, ion exchange chromatography and gel filtration. The determined molecular weight of the purified enzyme was about 95,000 by gel filtration and 100,000 daltons on SDS-polyacryamide gel electrophoresis. This enzyme didn´t show any activity change by several metal ions except 15.4% decrease by Mn^(2+) and was strongly inhibited by 2-mercaptoethanol and SDS. The invertase maintained its activity at high level until 70℃, but inactivated at 80℃ almost completely. The optimal temperature and pH of the enzyme were about 60℃ and pH 5.0, respectively. The stable pH range of invertase was narrow from pH 3.0 to 6.0. The Km value and isoeletric point of enzyme were 3.4×10 ³M, pH 5.5, respectively.
목차
Abstract
INTRODUCTION
MATERIALS AND METHODS
RESULT AND DISCUSSION
ACKNOWLEDGEMENTS
REFERENCES
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