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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.
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页数:12
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