流变学
纤维
吸附
化学工程
化学
下降(电信)
微观结构
不稳定
材料科学
结晶学
复合材料
有机化学
生物化学
工程类
社会心理学
电信
计算机科学
心理学
作者
Zhili Wan,Xiao‐Quan Yang,Leonard M.C. Sagis
出处
期刊:Langmuir
[American Chemical Society]
日期:2016-07-25
卷期号:32 (32): 8092-8101
被引量:118
标识
DOI:10.1021/acs.langmuir.6b01511
摘要
When soy glycinin (11S) is heated for a prolonged time at pH 2 (20 h at 85 °C), a mixture is formed consisting of long semiflexible 11S fibrils and small peptides. The surface and foaming properties of this mixture were investigated at different pHs, and compared to the behavior of pure fibrils and pure peptides, to determine the individual contributions of these two factions to the behavior of the mixture. The adsorption of these three systems at air-water interfaces and the resulting surface rheological properties were studied by combining drop shape analysis tensiometry, ellipsometry, and surface large amplitude oscillatory dilatational (LAOD) rheology. Lissajous plots of surface pressure versus deformation were used to analyze the surface rheological response in terms of interfacial microstructure. Our results show that the adsorption kinetics, dilatational rheological properties, and the foaming behavior of the mixture were mainly dominated by the small peptides in the fibril system. Compared to pH 2, the fibril mixture at pH 5 and 7 provides much better foam stability and appears to be a very promising protein material to make stable foams, even at low protein concentration (0.1 wt %). The presence of fibril clusters and peptide aggregates at pH 5 and 7 contributed to foam stability of the mixture. In contrast, pure fibril formed an interface with a highly pH-responsive adsorption and rheological behavior, and the foamability and foam stability of the pure fibrils were very poor.
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