Functionality of lupin seed protein isolate in relation to its interfacial behaviour

被引：50
|
作者：
Pozani, S [1 ]
Doxastakis, G [1 ]
Kiosseoglou, V [1 ]
机构：
[1] Aristotelian Univ Thessaloniki, Fac Chem, Food Chem & Technol Lab, Thessaloniki 54006, Greece
来源：
FOOD HYDROCOLLOIDS | 2002年 / 16卷 / 03期
关键词：
lupin seed protein isolate; functional properties; interfacial activity;
D O I：
10.1016/S0268-005X(01)00094-7
中图分类号：
O69 [应用化学];
学科分类号：
081704 ;
摘要：
The foaming and emulsifying properties of lupin seed protein isolate (LSPI) were investigated following protein structure modification by heating and/or dithiothreitol (DTT) addition. Heat-treatment of protein solution resulted in an increase of both foamability and foam-stabilization ability while disulfide bond reduction by DTT brought about an improvement in the protein foaming capacity only. Additionally, heat-treated LSPI solutions exhibited markedly improved emulsification and emulsion-stabilization properties. Disulfide bond reduction, on the other hand, brought about an increase in the ability of the protein to stabilize the emulsions against creaming only. The influence of lupin protein structure modification on its solubility and surface-adsorption properties has also been studied in order to elucidate the protein structure/functionality relationship of lupin protein. (C) 2002 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码：241 / 247
页数：7
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