Interpolymeric complexing between egg white proteins and xanthan gum: Effect of salt and protein/polysaccharide ratio

被引:126
|
作者
Souza, Clitor J. F. [1 ]
Garcia-Rojas, Edwin E. [1 ,2 ]
机构
[1] UFRRJ, PPGCTA, Rodovia BR 465 Km 7, BR-23890000 Seropedica, RJ, Brazil
[2] Univ Fed Fluminense, LETA, Ave Trabalhadores 420, BR-27255125 Volta Redonda, RJ, Brazil
关键词
Lysozyme; Ovalbumin; Interpolymeric complex; Rheology; Electrostatic interactions; IONIC-STRENGTH; RHEOLOGICAL PROPERTIES; SECONDARY STRUCTURE; BETA-LACTOGLOBULIN; WHEY PROTEINS; COACERVATION; PH; POLYELECTROLYTES; COMPLEXATION; DISSOCIATION;
D O I
10.1016/j.foodhyd.2016.11.032
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
The aim of this work was to characterize the complexes lysozyme (Lyso)/xanthan gum (XG) and ovalbumin (Ova)/xanthan gum in terms of their physicochemical properties and to study the influence of salt and protein/polysaccharide ratio on rheological properties. As the protein/polysaccharide ratio was increased from 1:1 to 10:1, critical structure events shifted to higher pHs, resulting in the formation of insoluble complexes even at pH 12.0. Lyso/XG complex formed a stronger gel-like complex with smaller loss tangents compared with the Ova/XG complex; however, those gels showed a slight tendency to breakdown under higher frequency variation when compared with Ova/XG complex. The correlation between rheological data, the effect of ionic strength and FTIR analysis suggests that although an electrostatic interaction is the main mechanism of interaction between biopolymers, non-electrostatic interactions also plays a role in the strength of the interaction. Egg white protein/XG complexes represent a great technological to formulate functional hydrogels. (C) 2016 Elsevier Ltd. All rights reserved.
引用
收藏
页码:268 / 275
页数:8
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