Korean Journal of Food Science and Technology (한국식품과학회지)
- Volume 21 Issue 4
- /
- Pages.569-574
- /
- 1989
- /
- 0367-6293(pISSN)
Purification and Characterization of Kiwifruit Protease
키위열매 Protease 의 추출 정제 및 그 특성에 대하여
- Kim, Bok-Ja (Dept. of Food and nutrition, Dae Jeon Junior College)
- 김복자 (대전실업전문대학 식품영양과)
- Published : 1989.08.01
Abstract
These studies were conducted to investigate the purification and characterization of Kiwifruit protease, and the results obtained were as follows The protease was purified by ammonium sulfate fractionation, Sephadex G-100 filtration and DEAE-Sephadex A-50 column chromatography and purified enzyme gave a single protein band on polyacrylamide gel electrophoresis The specific activity of purified enzyme was 30,10 units/mg protein and the yield was 7.48. The purified enzyme showed a high affinity for casein and hemoglobin. The optimal pH and temperature for enzyme activity were 7.0 and
Kiwifruit에서 pretense를 추출 정제하여 그의 특성을 검토하였다. 조효소는 유안분획, sephadex G-100 filtration 및 DEAE-sephadex A-50 column chromatography를 거쳐 정제되었으며 정제효소의 비활성은 30.10으로 10.95배 증가하였고 활성수율은 7.48%에 달하였다. 정제효소는 casein및 hemoglobin을 잘 분해하였고 작용 최적 pH는 7.0이었으며 pH
Keywords