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.

引用

页码：359 / 362

页数：4

共 16 条

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