Spontaneous gelation of wheat gluten proteins in a food grade solvent

被引:36
作者
Dahesh, Mohsen [1 ,2 ]
Banc, Amelie [1 ]
Duri, Agnes [2 ]
Morel, Marie-Helene [2 ]
Ramos, Laurence [1 ]
机构
[1] Univ Montpellier, CNRS, Lab Charles Coulomb L2C, UMR 5221, F-34059 Montpellier, France
[2] UM2 CIRAD INRA SupAgro, UMR IATE, F-34070 Montpellier, France
关键词
Near critical gel; Protein; Gluten; Hydrogen bonding; Fractal dimension; Percolation; GEL POINT; CROSS-LINKING; VISCOELASTIC PROPERTIES; LINEAR VISCOELASTICITY; RHEOLOGY; SHEAR; POWER; MECHANISM; NETWORKS; HEAT;
D O I
10.1016/j.foodhyd.2015.06.014
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
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.
引用
收藏
页码:1 / 10
页数:10
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