文献类型：期刊文献

英文题名：Binding of (-)-epigallocatechin-3-gallate with thermally-induced bovine serum albumin/ι-carrageenan particles

作者：Li, Jinbing[1];Wang, Xiaoyong[1]

机构：[1]E China Univ Sci & Technol, Sch Chem & Mol Engn, Shanghai 200237, Peoples R China

年份：2015

卷号：168

起止页码：566

外文期刊名：FOOD CHEMISTRY

收录：;EI(收录号：20143418081061);WOS:【SCI-EXPANDED(收录号:WOS:000343612800075)】；

基金：Financial support from the National Natural Science Foundation of China (Grant 21173081) and the Fundamental Research Funds for the Central Universities (Grant WK1213003) is gratefully acknowledged.

语种：英文

外文关键词：Biopolymer particles; EGCG; Fluorescence; Binding constant; Stability

摘要：Novel thermally-induced BSA/iota-carrageenan particles are used as a protective carrier for (-)-epigallocatechin-3-gallate (EGCG). The addition of EGCG to BSA/iota-carrageenan particles can highly quench the intrinsic fluorescence of BSA, which is explained in terms of the binding of EGCG to the hydrophobic pockets of BSA mainly through the hydrophobic force. According to the double logarithm equation, the binding constant is determined as 1.1 x 10(8) M-1 for the binding of EGCG with BSA/iota-carrageenan particles. The high binding affinity is ascribed to both the molecular structure of EGCG and the partial unfolding state of BSA in BSA/iota-carrageenan particles. The circular dichroism spectra and calculated a-helix of BSA suggest that the bound EGCG leads to a more random secondary structure of BSA. Furthermore, BSA/iota-carrageenan particles are found to be superior to native BSA and pure BSA particles for improving the stability and radical scavenging activity of EGCG. (C) 2014 Elsevier Ltd. All rights reserved.