Spontaneous gelation of wheat gluten proteins in a food grade solvent
Spontaneous gelation of wheat gluten proteins in a food grade solvent
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DOI：
10.1016/j.foodhyd.2015.06.014
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发表时间：
2016-01-01
影响因子：
10.7
通讯作者：
Ramos, Laurence
中科院分区：
文献类型：
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作者：
Dahesh, Mohsen;Banc, Amelie;Ramos, Laurence
将小麦面筋蛋白结构化为具有可调机械性质的凝胶将为生产富含植物蛋白的食品提供更多的通用性。面筋是一种不溶于水的强弹性蛋白质材料，很难加工。我们使用一种新的分馏程序，允许从面筋的水/乙醇可溶性蛋白质混合物，富含谷蛋白聚合物在前所未有的高比例（50%）的分离。我们在这里调查的蛋白质混合物在水/乙醇（50/50 v/v）溶剂中的悬浮液的粘弹性，并表明，在很宽的浓度范围内，它们经历了由氢键驱动的自发凝胶化。我们成功地合理化我们的数据，使用渗流模型和相关的凝胶的粘弹性，其分形维数测量散射技术。谷蛋白凝胶显示出自修复特性，并且其弹性平台覆盖几十年，从0.01到10，000 Pa。特别地，可以生产与标准水合面筋相比非常软的凝胶。(C)2015爱思唯尔有限公司版权所有。
Structuring wheat gluten proteins into gels with tunable mechanical properties would provide more versatility for the production of plant protein-rich food products. Gluten, a strongly elastic protein material insoluble in water, is hardly processable. We use a novel fractionation procedure allowing the isolation from gluten of a water/ethanol soluble protein blend, enriched in glutenin polymers at an unprecedented high ratio (50%). We investigate here the viscoelasticity of suspensions of the protein blend in a water/ethanol (50/50 v/v) solvent, and show that, over a wide range of concentrations, they undergo a spontaneous gelation driven by hydrogen bonding. We successfully rationalize our data using percolation models and relate the viscoelasticity of the gels to their fractal dimension measured by scattering techniques. The gluten gels display self-healing properties and their elastic plateaus cover several decades, from 0.01 to 10,000 Pa. In particular very soft gels as compared to standard hydrated gluten can be produced. (C) 2015 Elsevier Ltd. All rights reserved.