Interaction between Vaccinium bracteatum Thunb. leaf pigment and rice proteins

被引：23

作者：

Wang, Li ^{[1
]}

Xu, Yuan ^{[1
]}

Zhou, Sumei ^{[2
]}

Qian, Haifeng ^{[1
]}

Zhang, Hui ^{[1
]}

Qi, Xiguang ^{[1
]}

Fan, Meihua ^{[3
]}

机构：

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

[2] Chinese Acad Agr Sci, Inst Food Sci & Technol, Beijing 100193, Peoples R China

[3] Jiangsu Inst Poultry Sci, Yangzhou 225125, Jiangsu, Peoples R China

来源：

FOOD CHEMISTRY | 2016年 / 194卷

关键词：

Vaccinium bracteatum Thunb; Rice protein; Surface hydrophobicity; Secondary structure; Hydrophobic interaction; Hydrogen bonding; ANTIOXIDANT ACTIVITY; POLYPHENOLS; LEAVES; ANTHOCYANINS; FLAVONOIDS; CAPACITY; CASEIN; JUICE;

D O I：

10.1016/j.foodchem.2015.08.006

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

In this study, we investigated the interaction of Vaccinium bracteatum Thunb. leaf (VBTL) pigment and rice proteins. In the presence of rice protein, VBTL pigment antioxidant activity and free polyphenol content decreased by 67.19% and 68.11%, respectively, and L* of the protein-pigment complex decreased significantly over time. L* values of albumin, globulin and glutelin during 60-min pigment exposure decreased by 55.00, 57.14, and 54.30%, respectively, indicating that these proteins had bound to the pigment. A significant difference in protein surface hydrophobicity was observed between rice proteins and pigment-protein complexes, indicating that hydrophobic interaction is a major binding mechanism between VBTL pigment and rice proteins. A significant difference in secondary structures between proteins and protein-pigment complexes was also uncovered, indicating that hydrogen bonding may be another mode of interaction between VBTL pigment and rice proteins. Our results indicate that VBTL pigment can stain rice proteins with hydrophobic and hydrogen interactions. (C) 2015 Elsevier Ltd. All rights reserved.

引用

页码：272 / 278

页数：7

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