Impacts of Proanthocyanidin Binding on Conformational and Functional Properties of Decolorized Highland Barley Protein
Juan Li,
Xin Zhang,
Wenju Zhou,
Zhaoxin Tu,
Xijuan Yang,
Jing Hao,
Feng Liang,
Zhengxing Chen,
Yan Du
Affiliations
Juan Li
National Engineering Research Center of Cereal Fermentation and Food Biomanufacturing, Jiangnan University, Wuxi 214122, China
Xin Zhang
National Engineering Research Center of Cereal Fermentation and Food Biomanufacturing, Jiangnan University, Wuxi 214122, China
Wenju Zhou
Qinghai Tianyoude Technology Investment Management Group Co., Ltd., Qinghai Engineering Technology Research Institute for Comprehensive Utilization of Highland Barley Resources, Xining 810016, China
Zhaoxin Tu
Qinghai Tianyoude Technology Investment Management Group Co., Ltd., Qinghai Engineering Technology Research Institute for Comprehensive Utilization of Highland Barley Resources, Xining 810016, China
Xijuan Yang
Qinghai Tibetan Plateau Key Laboratory of Agric-Product Processing, Qinghai Academy of Agricultural and Forestry Sciences, Xining 810016, China
Jing Hao
Qinghai Tianyoude Technology Investment Management Group Co., Ltd., Qinghai Engineering Technology Research Institute for Comprehensive Utilization of Highland Barley Resources, Xining 810016, China
Feng Liang
Qinghai Tianyoude Technology Investment Management Group Co., Ltd., Qinghai Engineering Technology Research Institute for Comprehensive Utilization of Highland Barley Resources, Xining 810016, China
Zhengxing Chen
National Engineering Research Center of Cereal Fermentation and Food Biomanufacturing, Jiangnan University, Wuxi 214122, China
Yan Du
National Engineering Research Center of Cereal Fermentation and Food Biomanufacturing, Jiangnan University, Wuxi 214122, China
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 β-sheets, a decrease in the number of α-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.
