Complexation of rice proteins and whey protein isolates by structural interactions to prepare soluble protein composites

被引：87

作者：

Wang, Ren ^{[1
,2
,3
,4
]}

Xu, Pengcheng ^{[1
,2
,3
,4
]}

Chen, Zhengxing ^{[1
,2
,3
,4
]}

Zhou, Xing ^{[1
,2
]}

Wang, Tao ^{[1
,2
,3
,4
]}

机构：

[1] Jiangnan Univ, State Key Lab Food Sci & Technol, Wuxi 214122, Peoples R China

[2] Jiangnan Univ, Natl Engn Lab Cereal Fermentat Technol, Wuxi 214122, Peoples R China

[3] Jiangnan Univ, Jiangsu Prov Res Ctr Bioact Prod Proc Technol, Wuxi 214122, Peoples R China

[4] Jiangnan Univ, Sch Food Sci & Technol, Wuxi 214122, Peoples R China

来源：

LWT-FOOD SCIENCE AND TECHNOLOGY | 2019年 / 101卷

基金：

中国国家自然科学基金;

关键词：

Rice proteins; Whey protein isolates; Solubility; Structural interactions; FUNCTIONAL-PROPERTIES; BRAN PROTEIN; EXTRACTION; MECHANISMS;

D O I：

10.1016/j.lwt.2018.11.006

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

The main factor limiting the preparation of high value-added rice proteins (RPs) is their low solubility. In this experiment, whey protein isolates (WPIs), which are of high nutritional value, were compounded with RPs at pH 12, and formed RP-WPI complexes by neutralization to pH 7 (pH-cycle). The formation of the protein complexes was studied by fluorescence and ultraviolet (UV) spectra. The results showed that hydrogen bond, hydrophobic force and electrostatic interaction mediated the merging of the two proteins into particulate spheres. Meanwhile the complexes acquired considerable surface charges resisting aggregation of the protein bodies, and the solubility of RPs was increased to more than 50%. The effectiveness of protein interactions by pH-cycle used in this study indicated that the technique may be a versatile approach to improve the functional properties of food proteins.

引用

页码：207 / 213

页数：7

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