Use of polysaccharides to control protein adsorption to the air-water interface

被引:73
|
作者
Ganzevles, RA
Stuart, MAC
van Vliet, T
de Jongh, HHJ
机构
[1] Univ Wageningen & Res Ctr, Dept Agrotechnol & Food Sci, Lab Phys Chem & Colloid Sci, NL-6700 EK Wageningen, Netherlands
[2] Wageningen Ctr Food Sci, NL-6700 AN Wageningen, Netherlands
[3] Univ Wageningen & Res Ctr, Dept Agrotechnol & Food Sci, NL-6700 EV Wageningen, Netherlands
[4] TNO, Qual Life, NL-3700 AJ Zeist, Netherlands
关键词
beta-lactoglobulin; pectin; electrostatic interaction; adsorption kinetics; air-water interface; foam formation;
D O I
10.1016/j.foodhyd.2005.08.009
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
In order to understand foaming behaviour of mixed protein/anionic polysaccharide solutions, we investigated the effect of beta-lactoglobulin/pectin interaction in the bulk on beta-lactoglobulin adsorption to the air-water interface. Adsorption kinetics were evaluated by following surface pressure development in time of several pure protein solutions and of mixed protein/polysaccharide solutions using an automated drop tensiometer (ADT). It was found that complexation of proteins with polysaccharides can slow down the kinetics of surface pressure development by at least a factor 100; and greatly diminish foam formation. In contrast, a five times acceleration in the increase of surface pressure was observed in other cases. We propose a mechanism for protein adsorption from mixed protein/polysaccharide solutions. Effects of ionic strength, pH and mixing ratio on this mechanism were studied for mixtures of beta-lactoglobulin and low methoxyl pectin, whereas other proteins and anionic polysaccharides were used to explore the role of protein and polysaccharide charge density and distribution. Whereas the possibilities to change system parameters like ionic strength or pH are limited in food related systems, selecting a suitable combination of protein and polysaccharide offers a broad opportunity to control protein adsorption kinetics and with that foam formation. (c) 2005 Elsevier Ltd. All rights reserved.
引用
收藏
页码:872 / 878
页数:7
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