Chemistry of gluten proteins
Chemistry of gluten proteins
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DOI：
10.1016/j.fm.2006.07.004
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发表时间：
2007-04-01
影响因子：
5.3
通讯作者：
Wieser, Herbert
中科院分区：
文献类型：
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作者：
Wieser, Herbert
面筋蛋白通过赋予面团吸水能力、黏性、粘度和弹性，在决定小麦独特的烘焙品质中起着关键作用。面筋蛋白根据其在水醇中的溶解度可分为两大类：可溶性麦胶蛋白和不溶性麦胶蛋白。这两个部分都含有大量的，部分密切相关的蛋白质成分，其特征是谷氨酰胺和脯氨酸含量高。麦胶蛋白主要是单体蛋白，分子量（Mws）在28000 - 55000之间，根据其初级结构的不同可分为α / β -型、γ -型和ω -型。二硫键要么不存在，要么以链内交联的形式存在。谷蛋白部分包括通过链间二硫键连接的聚集蛋白；它们的规模从大约50万到1000多万不等。二硫键还原后，得到的谷蛋白亚基在醇水溶液中的溶解度与麦胶蛋白相似。根据初级结构，谷蛋白亚基可分为高分子量（HMW）亚基（MW = 67,000-88,000）和低分子量（LMW）亚基（MW = 32,000-35,000）。每一种面筋蛋白类型由两到三个不同的结构域组成；其中一个含有独特的富含谷氨酰胺和脯氨酸的重复序列。天然谷蛋白是由HMW亚基聚合物和由HMW亚基分支的LMW亚基聚合物组成的主链。氢键、离子键和疏水键等非共价键对麦胶蛋白和谷蛋白的聚集起着重要的作用，并影响着面团的结构和物理性质。(c) 2006 Elsevier Ltd.版权所有。
Gluten proteins play a key role in determining the unique baking quality of wheat by conferring water absorption capacity, cohesivity, viscosity and elasticity on dough. Gluten proteins can be divided into two main fractions according to their solubility in aqueous alcohols: the soluble gliadins and the insoluble glutenins. Both fractions consist of numerous, partially closely related protein components characterized by high glutamine and proline contents. Gliadins are mainly monomeric proteins with molecular weights (Mws) around 28,000-55,000 and can be classified according to their different primary structures into the alpha/beta-, gamma- and omega-type. Disulphide bonds are either absent or present as intrachain crosslinks. The glutenin fraction comprises aggregated proteins linked by interchain disulphide bonds; they have a varying size ranging from about 500,000 to more than 10 million. After reduction of disulphide bonds, the resulting glutenin subunits show a solubility in aqueous alcohols similar to gliadins. Based on primary structure, glutenin subunits have been divided into the high-molecular-weight (HMW) subunits (MW = 67,000-88,000) and low-molecular-weight (LMW) subunits (MW = 32,000-35,000). Each gluten protein type consists or two or three different structural domains; one of them contains unique repetitive sequences rich in glutamine and proline. Native glutenins are composed of a backbone formed by HMW subunit polymers and of LMW subunit polymers branched off from HMW subunits. Non-covalent bonds such as hydrogen bonds, ionic bonds and hydrophobic bonds are important for the aggregation of gliadins and glutenins and implicate structure and physical properties of dough. (c) 2006 Elsevier Ltd. All rights reserved.