Emulsifying and foaming properties of β-lactoglobulin modified by heat treatment

被引:46
作者
Moro, Andrea [1 ]
Baez, German D. [1 ]
Ballerini, Griselda A. [1 ,2 ]
Busti, Pablo A. [1 ]
Delorenzi, Nestor J. [1 ]
机构
[1] Univ Nacl Rosario, Area Fisicoquim, Dept Quim Fis, Fac Ciencias Bioquim & Farmaceut, RA-2000 Rosario, Santa Fe, Argentina
[2] Univ Tecnol Nacl, Ctr Invest & Desarrollo Tecnol Alimentos, Fac Reg Rosario, RA-2000 Rosario, Santa Fe, Argentina
关键词
Beta-lactoglobulin; Heating treatment; Protein aggregates; Foaming properties; Emulsifying properties; CREAMING STABILITY; SODIUM CASEINATE; MILK PROTEIN; EMULSIONS; INTERFACES; BOVINE; HYDROCOLLOIDS; KINETICS;
D O I
10.1016/j.foodres.2012.11.011
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The effects of heat treatment on emulsifying properties of beta-lactoglobulin were studied in order to compare them with previous studies on foaming properties. Both of them are closely linked to the structural changes on the protein. Aliquots from 5.5% (w/v) beta-lactoglobulin solution in 20 mM phosphate buffer at pH 6.8 were heated at 85 degrees C for different time periods, from 1 to 15 min. Protein solubilities were measured for unheated and heated beta-lactoglobulin samples. Protein-stabilized O/W emulsions were prepared with these samples and corn oil. Droplet size distribution in the emulsions and emulsifying activity index were determined for each system, as parameters of the emulsifying ability of the protein. Emulsion stability was estimated from three different methods: backscattering, determination of the remaining protein concentration after creaming and monitoring the oiling off process. With the assayed methodology, heat treatment of beta-lactoglobulin led to different effects on foaming and emulsifying properties of the protein, depending on the time of heating. For shorter times of heating, both foamability and foam stability improved, while emulsifying properties diminished. After 10 min of heating at 85 degrees C, both foaming and emulsifying properties diminished. Formation time scales, as well as size of the sedimentable aggregates and their steric effect on the interfacial film, play an important role in explaining these differences between foaming and emulsifying properties. (C) 2012 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1 / 7
页数:7
相关论文
共 34 条
[1]   DETERMINATION OF INTERFACIAL-AREAS IN EMULSIONS USING TURBIDIMETRIC AND DROPLET SIZE DATA - CORRECTION OF THE FORMULA FOR EMULSIFYING ACTIVITY INDEX [J].
CAMERON, DR ;
WEBER, ME ;
IDZIAK, ES ;
NEUFELD, RJ ;
COOPER, DG .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1991, 39 (04) :655-659
[2]  
Cayot P., 1997, FOOD PROTEINS THEIR, P473
[3]   Creaming stability of oil in water (O/W) emulsions:: Influence of pH on soybean protein-lecithin interaction [J].
Comas, D. I. ;
Wagner, J. R. ;
Tomas, M. C. .
FOOD HYDROCOLLOIDS, 2006, 20 (07) :990-996
[4]   Conformations and structures of milk proteins adsorbed to oil-water interfaces [J].
Dalgleish, DG .
FOOD RESEARCH INTERNATIONAL, 1996, 29 (5-6) :541-547
[5]  
Damodaran S, 2005, J FOOD SCI, V70, pR54
[6]  
DAMODARAN S, 1994, IFT BAS SYM, V9, P1
[7]   Hydrocolloids at interfaces and the influence on the properties of dispersed systems [J].
Dickinson, E .
FOOD HYDROCOLLOIDS, 2003, 17 (01) :25-39
[8]   Milk protein interfacial layers and the relationship to emulsion stability and rheology [J].
Dickinson, E .
COLLOIDS AND SURFACES B-BIOINTERFACES, 2001, 20 (03) :197-210
[9]  
DICKINSON E, 1992, INTRO FOOD COLLOIDS, P66
[10]   Hydrocolloids as emulsifiers and emulsion stabilizers [J].
Dickinson, Eric .
FOOD HYDROCOLLOIDS, 2009, 23 (06) :1473-1482