Interaction between plant phenolics and rice protein improved oxidative stabilities of emulsion

被引：52

作者：

Jia, Xiao ^{[1
,2
]}

Zhao, Mouming ^{[1
,3
]}

Xia, Ning ^{[1
]}

Teng, Jianwen ^{[1
]}

Jia, Chunxiao ^{[1
]}

Wei, Baoyao ^{[1
]}

Huang, Li ^{[1
]}

Chen, Dewei ^{[1
]}

机构：

[1] Guangxi Univ, Coll Light Ind & Food Engn, Nanning 530004, Peoples R China

[2] Chinese Acad Agr Sci, Oil Crops Res Inst, Wuhan 430062, Hubei, Peoples R China

[3] South China Univ Technol, Sch Food Sci & Engn, Guangzhou 510640, Guangdong, Peoples R China

来源：

JOURNAL OF CEREAL SCIENCE | 2019年 / 89卷

基金：

中国国家自然科学基金;

关键词：

Rice protein; Ferulic acid; Emulsion; Oil; Oxidation stability; LIPID OXIDATION; ANTIOXIDANT PROPERTIES; BINDING INTERACTION; CHLOROGENIC ACID; FERULIC ACID; WHEY; INHIBITION; GLUTELIN; AMYLASE; BRAN;

D O I：

10.1016/j.jcs.2019.102818

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

The interaction between rice protein isolate (RPI) and ferulic acid (FA) was systematically investigated. The results showed that fluorescence intensity of the RPI decreased gradually upon increasing the concentration of ferulic acid, and the maximum emission shifted from 352.0 to 359.2 nm. It was proposed that a static quenching of RPI-FA complex occurred, due to the hydrophobic interactions. Moreover, CD spectra and FT-IR spectroscopy data suggested that the concentration of beta-turn and alpha-helix decreased while those of random coil and beta-sheet increased in RPI-FA complex. The decrease of intensity of the amide I band and amide II band in the RN-FA complex implied a significant reduction of protein alpha-helical structure and the presence of non-polar hydrophobic interactions. In addition, SDS-PAGE results demonstrated that ferulic acid reacted with glutelin acidic subunits (34-37 KDa) as well as globulin (26 KDa), and ferulic acid might bind with aromatic amino acid residues of RPI. Furthermore, the RPI-FA complex exhibited high DPPH center dot scavenging ability, ABTS(+)center dot scavenging ability and ORAC value. Finally, emulsion stabilized by RPI-FA complex could decrease the concentration of hydroperoxide, TBARS, and hexanal, thereby effectively restraining fat oxidation degradation.

引用

页数：7

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