SOLUBILITY AND ENZYMATIC SOLUBILIZATION OF MUSCLE AND SKIN OF CAPELIN (MALLOTUS-VILLOSUS) AT DIFFERENT PH AND TEMPERATURE

被引：15

作者：

GILDBERG, A ^{[1
]}

RAA, J ^{[1
]}

机构：

[1] UNIV TROMSO,N-9000 TROMSO,NORWAY

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1979年 / 63卷 / 03期

关键词：

D O I：

10.1016/0305-0491(79)90254-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

1. 1. The breaking strength of capelin skin increases in the pH range from 6 to 10. 2. 2. Digestive enzymes in capelin degrade protein in the native skin at pH below 6, but not at neutral or alkaline conditions. 3. 3. The digestive enzymes release proteins with high molecular weight when acting on muscle tissue at neutral pH. 4. 4. Adjusting the pH to 4 facilitates a chemical/enzymatic dissection of skin and myocommata and simultaneously minimizes solubilization of muscle protein. © 1979.

引用

页码：309 / 314

页数：6

共 11 条

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