School of Plant Biology, Faculty of Natural and Agricultural Sciences and The UWA Institute of Agriculture, The University of Western Australia, 35 Stirling Highway, Crawley, WA 6009, Australia.
J Agric Food Chem. 2011 Jun 22;59(12):6696-704. doi: 10.1021/jf201293p. Epub 2011 May 24.
Bread made from a mixture of wheat and lupin flour possesses a number of health benefits. The addition of lupin flour to wheat flour during breadmaking has major effects on bread properties. The present study investigated the lupin and wheat flour protein interactions during the breadmaking process including dough formation and baking by using proteomics research technologies including MS/MS to identify the proteins. Results revealed that qualitatively most proteins from both lupin and wheat flour remained unchanged after baking as per electrophoretic behavior, whereas some were incorporated into the bread gluten matrix and became unextractable. Most of the lupin α-conglutins could be readily extracted from the lupin-wheat bread even at low salt and nonreducing/nondenaturing extraction conditions. In contrast, most of the β-conglutins lost extractability, suggesting that they were trapped in the bread gluten matrix. The higher thermal stability of α-conglutins compared to β-conglutins is speculated to account for this difference.
由小麦和羽扇豆混合面粉制成的面包具有许多健康益处。在面包制作过程中，向小麦粉中添加羽扇豆粉会对面包的特性产生重大影响。本研究通过使用包括 MS/MS 在内的蛋白质组学研究技术，研究了面包制作过程中羽扇豆和小麦粉蛋白质的相互作用，包括面团形成和烘焙。结果表明，根据电泳行为，烘焙后大多数来自羽扇豆和小麦粉的蛋白质在质量上保持不变，而有些则被掺入面包面筋基质中并变得不可提取。即使在低盐和非还原/非变性提取条件下，大多数羽扇豆α-聚集蛋白也可以很容易地从羽扇豆-小麦面包中提取出来。相比之下，大多数β-聚集蛋白失去了可提取性，表明它们被困在面包面筋基质中。与β-聚集蛋白相比，α-聚集蛋白的热稳定性更高，据推测这就是造成这种差异的原因。
