Tilley K A, Benjamin R E, Bagorogoza K E, Okot-Kotber B M, Prakash O, Kwen H
Department of Grain Science and Industry, 201 Shellenberger Hall, Kansas State University, Manhattan, Kansas 66506, USA.
J Agric Food Chem. 2001 May;49(5):2627-32. doi: 10.1021/jf010113h.
The formation of the large protein structure known as "gluten" during dough-mixing and bread-making processes is extremely complex. It has been established that a specific subset of the proteins comprising gluten, the glutenin subunits, directly affects dough formation and breadmaking quality. Glutenin subunits have no definitive structural differences that can be directly correlated to their ability to form gluten and affect dough formation or breadmaking quality. Many protein structural studies, as well as mixing and baking studies, have postulated that disulfide bonds are present in the gluten structure and contribute to the process of dough formation through the process of disulfide-sulfhydryl exchange. Evidence presented here indicates that tyrosine bonds form in wheat doughs during the processes of mixing and baking, contributing to the structure of the gluten network. The relative contributions of tyrosine bonds and disulfide--sulfhydryl interchange are discussed.
在面团搅拌和面包制作过程中，被称为“面筋”的大型蛋白质结构的形成极为复杂。现已确定，构成面筋的特定蛋白质亚组，即麦谷蛋白亚基，直接影响面团的形成和面包制作质量。麦谷蛋白亚基没有明确的结构差异可直接与其形成面筋以及影响面团形成或面包制作质量的能力相关联。许多蛋白质结构研究以及搅拌和烘焙研究都推测，面筋结构中存在二硫键，并通过二硫键-巯基交换过程促进面团形成过程。此处提供的证据表明，在搅拌和烘焙过程中，小麦面团中会形成酪氨酸键，有助于面筋网络的结构。本文讨论了酪氨酸键和二硫键-巯基交换的相对作用。
