Extreme pH treatments enhance the structure-reinforcement role of soy protein isolate and its emulsions in pork myofibrillar protein gels in the presence of microbial transglutaminase

被引:219
|
作者
Jiang, Jiang [1 ,2 ]
Xiong, Youling L. [3 ]
机构
[1] Jiangnan Univ, State Key Lab Food Sci & Technol, Wuxi 214122, Jiangsu, Peoples R China
[2] Jiangnan Univ, Sch Food Sci & Technol, Wuxi 214122, Jiangsu, Peoples R China
[3] Univ Kentucky, Dept Anim & Food Sci, Lexington, KY 40546 USA
关键词
Myofibrillar proteins; Soy proteins; pH treatment; Emulsion; Gel; HEAT-INDUCED GELATION; CROSS-LINKING; EMULSIFYING PROPERTIES; RHEOLOGICAL PROPERTIES; FUNCTIONAL-PROPERTIES; SHIFTING PROCESSES; BETA-CONGLYCININ; MYOSIN; GLYCININ; FAT;
D O I
10.1016/j.meatsci.2012.11.002
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Alkali (pH(12)) and acid (pH(1.5)) pH-treated soy protein isolates (SPI) were incorporated (0.25-0.75% protein) into sols of myofibrillar protein (MP, 3%, in 0.6 M NaCl at pH 6.25) with or without 0.1% microbial transglutaminase (TG) to investigate the potential as meat processing ingredients. Static and dynamic theological measurements showed significant enhancements of MP gelling ability by the inclusion of pH(1.5)-treated as well as preheated SPI (90 degrees C, 3 min). A 7-h incubation with TG accentuated the gel-strengthening effect by these SPI samples. The B subunit in 11S of SPI was the main component manifesting structure reinforcement in the mixed gels. The MP gelling properties were also greatly improved (P<0.05) by the addition of 10% canola oil emulsions stabilized by pH-treated SPI. The principal force in the MP gels incorporated with pH-treated SPI was hydrophobic patches; in the presence of TG, cross-linking of previously dissociated A and B subunits of 11S was also intimately involved. (c) 2012 Elsevier Ltd. All rights reserved.
引用
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页码:469 / 476
页数:8
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