Effect of transglutaminase-induced cross-linking on gelation of myofibrillar/soy protein mixtures

被引:170
作者
Ramírez-Suárez, JC [1 ]
Xiong, YL [1 ]
机构
[1] Univ Kentucky, Dept Anim Sci, Food Sci Sect, Lexington, KY 40546 USA
关键词
transglutaminase; myofibrillar proteins; soy proteins; gelation;
D O I
10.1016/S0309-1740(02)00297-8
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Microbial transglutaminase (MTGase)-catalyzed interaction and gelation of mixed myofibrillar (MPI)/soy (SPI) protein isolates were investigated at varying ionic strengths and MPI:SPI ratios, with or without SPI being preheated (80 degreesC). MTGase treatments in deionized water converted myosin heavy chain and actin into lower molecular-weight polypeptides, which gradually diminished as the ionic strength increased up to 0.6 M NaCl. A reduced intensity in the electrophoretic bands of soy proteins (7S and 11S except the basic subunits) was observed in all treatments, suggesting cross-linking with MPI. The enzyme treatment slightly increased the thermal transition (denaturation) temperatures of MPI/SPI but greatly enhanced (P < 0.05) the elasticity of the mixed protein gels when compared with untreated samples, independent of incubation time. (C) 2003 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:899 / 907
页数:9
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