PURIFICATION AND SOME PROPERTIES OF SODOM-APPLE LATEX PROTEINASES

被引：8
作者：
AWORH, OC [1 ]
KASCHE, V [1 ]
APAMPA, OO [1 ]
机构：
[1] UNIV IBADAN,DEPT FOOD TECHNOL,IBADAN,NIGERIA
来源：
FOOD CHEMISTRY | 1994年 / 50卷 / 04期
关键词：
D O I：
10.1016/0308-8146(94)90204-6
中图分类号：
O69 [应用化学];
学科分类号：
081704 ;
摘要：
Two thiol-activated proteinases with isoelectric points (pIs approximately 9-9.5) were purified from sodom-apple latex by chromatography on Q-Sepharose and Superdex 200. Proteinase I had an estimated molecular weight of approximately 25 000 and proteinase II one of about 30 000. The proteinases degraded casein and azocoll, proteinase I having a lower specific activity than proteinase II. Proteinase I was most active at pH 8-10, with the optimum at about pH 8. Proteinase II was most active at pH 6-8, with the optimum at about pH 7.
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页码：359 / 362
页数：4
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