Interaction of milk whey protein with common phenolic acids

被引：75

作者：

Zhang, Hao ^{[1
,2
,3
]}

Yu, Dandan ^{[1
]}

Sun, Jing ^{[1
]}

Guo, Huiyuan ^{[3
]}

Ding, Qingbo ^{[4
]}

Liu, Ruihai ^{[5
]}

Ren, Fazheng ^{[1
]}

机构：

[1] China Agr Univ, Coll Food Sci & Nutr Engn, Beijing Lab Food Qual & Safety, Beijing 100083, Peoples R China

[2] Key Lab Funct Dairy, Beijing 100083, Peoples R China

[3] Beijing Higher Inst Engn Res Ctr Anim Prod, Beijing 100083, Peoples R China

[4] COFCO Ltd, Beijing 10020, Peoples R China

[5] Cornell Univ, Dept Food Sci, Ithaca, NY 14853 USA

来源：

JOURNAL OF MOLECULAR STRUCTURE | 2014年 / 1058卷

基金：

中国博士后科学基金;

关键词：

Whey protein; Phenolic acid; Binding mode; Fluorescence spectroscopy; CD; FTIR; HUMAN SERUM-ALBUMIN; FLUORESCENCE SPECTROSCOPY; ANTIOXIDANT CAPACITY; FUNCTIONAL FOODS; CATIONIC LIPIDS; BINDING; BIOAVAILABILITY; NEVADENSIN; DENDRIMERS; FRUIT;

D O I：

10.1016/j.molstruc.2013.11.009

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Phenolics-rich foods such as fruit juices and coffee are often consumed with milk. In this study, the interactions of alpha-lactalbumin and beta-lactoglobulin with the phenolic acids (chlorogenic acid, caffeic acid, ferulic acid, and coumalic acid) were examined. Fluorescence, CD, and FTIR spectroscopies were used to analyze the binding modes, binding constants, and the effects of complexation on the conformation of whey protein. The results showed that binding constants of each whey protein-phenolic acid interaction ranged from 4 x 10(5) to 7 x 10(6) M-n and the number of binding sites n ranged from 1.28 +/- 0.13 to 1.54 +/- 0.34. Because of these interactions, the conformation of whey protein was altered, with a significant reduction in the amount of a-helix and an increase in the amounts of beta-sheet and turn structures. (C) 2013 Elsevier B.V. All rights reserved.

引用

页码：228 / 233

页数：6

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