Dynamic adsorption and interfacial rheology of whey protein isolate at oil-water interfaces: Effects of protein concentration, pH and heat treatment

被引:61
|
作者
Zhou, Beibei [1 ,2 ]
Tobin, John T. [1 ]
Drusch, Stephan [2 ]
Hogan, Sean A. [1 ]
机构
[1] TEAGASC, Food Chem & Technol Dept, Food Res Ctr, Moorepk, Fermoy P61 C996, Cork, Ireland
[2] Tech Univ Berlin, Dept Food Technol & Food Mat Sci, Konigin Luise Str 22, D-14195 Berlin, Germany
关键词
Oil/water interface; Whey protein isolate; Pendant drop tensiometry; Du Nouy ring; Dynamic adsorption; Interfacial rheology; BOVINE BETA-LACTOGLOBULIN; ALPHA-LACTALBUMIN; EMULSIFYING PROPERTIES; OIL/WATER INTERFACE; LIQUID INTERFACES; THERMAL-DENATURATION; FOAM STABILITY; SERUM-ALBUMIN; SURFACE; KINETICS;
D O I
10.1016/j.foodhyd.2021.106640
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
The effects of bulk protein concentration, C-p, (0.01, 0.1, 1 wt%), pH (3, 4.7 and 7) and heat treatment (unheated or 95 degrees C for 30 min) on whey protein isolate (WPI) stabilized interfaces were examined. The interfacial pressure and shear rheology of WPI-stabilized sunflower oil-water (o/w) interfaces were characterized using a pendant drop tensiometer and a rheometer equipped with a Du Nouy ring. The rate of WPI adsorption was faster at higer C-p and pH 3. Heat-enhanced surface activity was more pronounced at pH 7 compared to pH 3 as a result of greater heat stability of WPI at acidic pH. The elastic modulus of WPI stabilized interfaces increased with Cp (<= 0.1 wt%). A further increase in C-p (to 1 wt%) resulted in monolayer collapse and weaker films. Non-heated (NHT) WPI formed less elastic interfacial films at pH 3 than at pH7. Heat treatment enhanced the elastic behavior of interfacial films with longer relaxation times. This may be associated with the formation of intermolecular beta-sheets. The knowledge gained on the nature of WPI-stabilized interfaces can be used to better understand the stability of dairy emulsions during subsequent processing, digestion or storage.
引用
收藏
页数:12
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