Gelation of mixed myofibrillar/wheat gluten proteins treated with microbial transglutaminase

被引:59
作者
Ramírez-Suárez, JC
Addo, K [1 ]
Xiong, YL
机构
[1] Univ Kentucky, Dept Nutr & Food Sci, Lexington, KY 40546 USA
[2] Ctr Invest Alimentac & Desarrollo, Phuket 83000, Thailand
[3] Univ Kentucky, Dept Anim & Food Sci, Lexington, KY 40546 USA
关键词
myofibrillar protein; gluten; transglutaminase; gelation;
D O I
10.1016/j.foodres.2005.04.004
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Gluten (Glu) and an acid-extracted protein fraction W) from wheat flour were mixed (1:1 ratio) with myofibrillar protein (MP) and treated with microbial transglutaminase (MTGase) to observe the effect on heat-induced gelation. Dynamic rheological properties and thermal denaturation patterns of treated samples were measured, respectively, with an oscillatory rheometer and a differential scanning calorimeter. The storage modulus (G') of control MP sample (no MTGase), with a value of 533 Pa at end of heating (77 degrees C, was not affected (P > 0.05) by Glu nor by AF. However, mixed protein samples after the MTGase treatment produced higher gel elasticity values that differed (P < 0.05) between samples (1355, 1700 and 1875 Pa at 77 degrees C for MP, MP/AF, and MP/Glu, respectively). The NIP sample underwent three endothermic transitions (peaking at 61.5, 68.0, and 78.5 degrees C) during thermal scan. The treatment with MTGase and/or addition of Glu or AF tended to lower the temperature for the first transition but raised the temperature for the third transition, suggesting possible interactions of the muscle with non-muscle proteins. Published by Elsevier Ltd.
引用
收藏
页码:1143 / 1149
页数:7
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