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

ABSTRACT: 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 foa

SUBMITTER: Li J 

PROVIDER: S-EPMC9914363 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature