Impacts of Proanthocyanidin Binding on Conformational and Functional Properties of Decolorized Highland Barley Protein

被引：5
作者：
Li, Juan [1 ,2 ]
Zhang, Xin [1 ,2 ]
Zhou, Wenju [3 ]
Tu, Zhaoxin [3 ]
Yang, Xijuan [4 ]
Hao, Jing [3 ]
Liang, Feng [3 ]
Chen, Zhengxing [1 ,2 ]
Du, Yan [1 ,2 ]
机构：
[1] Jiangnan Univ, Natl Engn Res Ctr Cereal Fermentat & Food Biomfg, Wuxi 214122, Peoples R China
[2] Jiangnan Univ, Jiangsu Prov Engn Res Ctr Bioact Prod Proc, Wuxi 214122, Peoples R China
[3] Qinghai Tianyoude Technol Investment Management Gr, Qinghai Engn Technol Res Inst Comprehens Utilizat, Xining 810016, Peoples R China
[4] Qinghai Acad Agr & Forestry Sci, Qinghai Tibetan Plateau Key Lab Agr Prod Proc, Xining 810016, Peoples R China
来源：
FOODS | 2023年 / 12卷 / 03期
关键词：
functional properties; decolorized protein; highland barley; proanthocyanidin; structural changes; ACID; COMPLEXES; ISOLATE;
D O I：
10.3390/foods12030481
中图分类号：
TS2 [食品工业];
学科分类号：
0832 ;
摘要：
The impacts of interaction between proanthocyanidin (PC) and decolorized highland barley protein (DHBP) at pH 7 and 9 on the functional and conformational changes in DHBP were investigated. It was shown that PC strongly quenched the intrinsic fluorescence of DHBP primarily through static quenching. PC and DHBP were mainly bound by hydrophobic interactions. Additionally, free sulfhydryl groups and surface hydrophobicity obviously decreased in DHBP after combining with PC. The zeta potential of DHBP-PC complexes at pH 7 increased significantly. A change in the structure of DHBP was caused by interactions with PC, resulting in an increase in the number of beta-sheets, a decrease in the number of alpha-helixes, and a spectral shift in the amide II band. Furthermore, the presence of PC enhanced the foaming properties and antioxidant activity of DHBP. Overall, this study suggests that DHBP-PC complexes at pH 7 could be designed as a stable additive, and illustrates the potential applications of DHBP-PC complexes in the food industry.
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页数：16
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