Chemical cross-linking and molecular aggregation of soybean protein during extrusion cooking at low and high moisture content

文献类型： 外文期刊

第一作者： Chen, Feng Liang

作者： Chen, Feng Liang;Wei, Yi Min;Zhang, Bo

作者机构：

关键词： Soybean protein;Extrusion texturization;Dead-stop operation;Protein solubility;Molecular aggregation

期刊名称：LWT-FOOD SCIENCE AND TECHNOLOGY （ 影响因子：4.952； 五年影响因子：5.383 ）

ISSN： 0023-6438

年卷期： 2011 年 44 卷 4 期

页码：

收录情况： SCI

摘要： Soybean protein isolate (SPI) was extruded using a co-rotating twin-screw extruder at low (28%) and high (60%) moisture content. Dead-stop operation was employed to obtain samples from different zones of the extruder. The protein solubility of extrudate was analyzed based on 8 different combinations of chemical bond-breaking solutions, which contained only phosphate buffer (P); two reagents, i.e. sodium dodecyl sulfate (SDS) in P (P + S), urea in P (P + U) and 2-mercaptoethanol (2-ME) in P (P + M); three reagents, i.e. (P + S + U), (P + U + M) and (P + M + S); four reagents, i.e. (P + S + U + M). Based on the protein solubility in the combined extraction solutions, each specific chemical bond and their interactions responsible for supporting the extrudate structure were further analyzed. The aggregation of protein subunits in extruded sample was investigated by using SDS-PAGE electrophoresis. The results showed that hydrophobic interactions, hydrogen bonds, disulfide bonds and their interactions collectively hold the structure of extrudate; and the importance of non-covalent bonds outweighs covalent bonds. Increasing feed moisture content could increase the interactions between disulfide bonds and hydrogen bonds and between disulfide bonds and hydrophobic interactions (p < 0.05), reduce the degree of aggregation and the difference in protein protein interactions and protein subunits among different zones within the extruder. Crown Copyright (C) 2010 Published by Elsevier Ltd. All rights reserved.

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