한국식품영양과학회지 (Journal of the Korean Society of Food Science and Nutrition)
- 제17권4호
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- Pages.348-357
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- 1988
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- 1226-3311(pISSN)
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- 2288-5978(eISSN)
고구마 Polyphenol Oxidase의 정제 및 특성
Purification and Characterization of Polyphenol Oxidase in Sweet Potato (Ipomoea batatas)
- 정수자 (부산여자전문대학 식품영양과)
- Chung, Soo-Ja (Dept. of Food and Nutrition, Pusan Womens' Junior College)
- 발행 : 1988.12.30
초록
갈변반응에 관여하는 polyphenol oxidase(PPO : EC 1.10.3.1)를 한국산 고구마(Ipomoea batatas, val : Hong-mi)로부터 추출하여 ammoniun sulfate 분획 및 DEAE-cellulose column chromatography법에 의하여 정제한 결과, 효소활동도는 23.1배였으며 enzyme activity 수율은 41.5%이었다. 이 효소는 일반 전기 영동법에 의하여 8개의 isozymes 으로, 또한 isolectric focusing에 의하여 pI가 각각 다른 12개의 isozymes으로 분리되었고 그 pI의 범위는 3.2-9.6이었으며, Isoelectric focusing에 의하여 분리된 각 isozyme의 specific activity는 6,000-46,700U/mg protein의 범위에 있었다. 고구마 중의 PPO는
The present work was undertaken to investigated the purification and characterization of polyphenol oxidase (PPO ; EC 1.10.3.1) in sweet potato, particularly the number of PPO isozymes, and PPO properties such as pH optimum, heat stability, substrate specificity, kinetics, and inhibitor studies. The purification achieved was 23.1 fold from crude extract with a yield of 41.5%. Eight PPO isozymes and twelve PPO isozymes were detected by disc polyacrylamide gel electrophoresis and isoelectric focusing, respectively. The specific activity of each isozyme separated by isoelectric focusing was in the range of
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