Department of Food Science and Nutrition, University of Minnesota, 1334 Eckles Ave., St. Paul, MN 55108, USA; Department of Biochemistry, Science Building, University of Cape Coast, Cape Coast, Ghana.
Department of Food Science and Nutrition, University of Minnesota, 1334 Eckles Ave., St. Paul, MN 55108, USA; Department of Food, Environmental and Nutritional Sciences, Università degli Studi di Milano, via G. Celoria 2, 20133 Milan, Italy.
Food Chem. 2018 Jul 1;253:255-261. doi: 10.1016/j.foodchem.2018.01.146. Epub 2018 Jan 31.
The effect of puroindolines (PINs) on structural characteristics of wheat proteins was investigated in Triticum turgidum ssp. durum (cv. Svevo) and Triticum aestivum (cv. Alpowa) and in their respective derivatives in which PIN genes were expressed (Soft Svevo) or the distal end of the short arm of chromosome 5D was deleted and PINs were not expressed (Hard Alpowa). The presence of PINs decreased the amount of cold-SDS extractable proteins and the accessibility of protein thiols to specific reagents, but resulted in facilitated solvation of gluten proteins, as detected by tryptophan fluorescence measurements carried out on minimally mixed flour/water mixtures. We propose that PINs and gluten proteins are interacting in the grain or flour prior to mixing. Hydrophobic interactions between PINs and some of the gluten proteins modify the pattern of interactions among gluten proteins, thus providing an additional mechanistic rationale for the effects of PINs on kernel hardness.
研究了麦醇溶蛋白（PINs）对硬质小麦（cv. Svevo）和普通小麦（cv. Alpowa）及其各自表达 PIN 基因的衍生品种（Soft Svevo）或 5D 染色体短臂末端缺失且不表达 PINs 的品种（Hard Alpowa）中小麦蛋白结构特性的影响。PINs 的存在减少了冷 SDS 可提取蛋白的量，以及蛋白质巯基对特定试剂的可及性，但通过对最小混合面粉/水混合物进行色氨酸荧光测量，发现面筋蛋白的溶解变得更容易。我们提出，PINs 和面筋蛋白在混合之前就在谷物或面粉中相互作用。PINs 和一些面筋蛋白之间的疏水相互作用改变了面筋蛋白之间相互作用的模式，从而为 PINs 对面团硬度的影响提供了额外的机制解释。
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