TEMPERATURE AND PH AFFECT TRANSGLUTAMINASE-CATALYZED SETTING OF CRUDE FISH ACTOMYOSIN

被引：58

作者：

JOSEPH, D ^{[1
]}

LANIER, TC ^{[1
]}

HAMANN, DD ^{[1
]}

机构：

[1] N CAROLINA STATE UNIV,DEPT FOOD SCI,RALEIGH,NC 27695

来源：

JOURNAL OF FOOD SCIENCE | 1994年 / 59卷 / 05期

关键词：

DYNAMIC THEOLOGY; CROSS LINKING; SURIMI; TRANSGLUTAMINASE; ACTOMYOSIN;

D O I：

10.1111/j.1365-2621.1994.tb08180.x

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Dynamic rheological properties of actomyosin from two species (Alaska pollock, Atlantic croaker) were monitored during preincubation (setting) at 25 degrees C and 37 degrees C, followed by programmed (1 degrees C/min) cooking to 77 degrees C. Added guinea pig liver transglutaminase enhanced gelation, as indicated by increases in both storage modulus (G') and percentage of polymerized myosin heavy chain (MHC). In the presence of added transglutaminase maximum G' and MHC polymerization occurred at the same conditions of pH and temperature which were optimum for setting of surimi pastes. This suggested that the transglutaminase-mediated setting reaction in surimi was constrained more by the conformation of the substrate (i.e., myosin) than by that of the enzyme.

引用

页码：1018 / &

共 27 条

[1] CROSS-LINKING OF WHEY-PROTEIN BY TRANSGLUTAMINASE [J].