Influence of internal interfacial area on nanosecond relaxation of wheat gluten proteins as probed by broadband ultrasonic spectroscopy

被引:7
作者
Fan, Y. [1 ]
Scanlon, M. G. [2 ]
Page, J. H. [1 ]
机构
[1] Univ Manitoba, Dept Phys & Astron, Winnipeg, MB R3T 2N2, Canada
[2] Univ Manitoba, Dept Food Sci, Winnipeg, MB R3T 2N2, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
Ultrasonic spectroscopy; Gluten proteins; Molecular relaxation; Interface; GAS CELL STABILIZATION; BREAD DOUGH; MECHANICAL-PROPERTIES; AIR/WATER INTERFACE; COMPUTED-TOMOGRAPHY; SECONDARY STRUCTURE; FOAMING PROPERTIES; REDUCED PRESSURE; PLANT PROTEIN; FLOUR DOUGHS;
D O I
10.1016/j.colsurfb.2013.05.032
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Understanding interactions between interfaces and biopolymers in complex industrially processed materials of plant origin will allow for their better utilization. Wheat flour doughs are one such material whose industrial use strongly depends on such interactions due to their effect on the mechanical properties of the dough. To date, mechanical characterizations of dough have been limited to a narrow range of frequencies. Here, ultrasonic spectroscopy measurements over a very broad frequency range are used to show that a fast volumetric relaxation occurs in dough; the nanosecond timescale of the relaxation is associated with ultrasonic stress-induced changes in the secondary structure of gluten proteins. Interestingly, there is a four-fold difference in the speed of this relaxation phenomenon in doughs mixed in air (where substantial internal interfacial area exists) compared to those mixed under vacuum (where bubbles are absent). Given the large internal interfacial area in dough, the amphiphilic proteins residing at gas bubble interfaces significantly alter the high-frequency mechanical response of this important material. (C) 2013 Elsevier B.V. All rights reserved.
引用
收藏
页码:466 / 473
页数:8
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