Interaction between Unfolded Bovine β-Lactoglobulin and Epigallocatechin Gallate

doi:10.7506/spkx1002-6630-20171212-141

Abstract

Abstract: The interaction mechanism of unfolded bovine β-lactoglobulin (U-β-LG) with epigallocatechin gallate (EGCG) was investigated by using fluorescence, ultraviolet and circular dichroism (CD) spectroscopy. U-β-LG was obtained after β-lactoglobulin (β-LG) was treated by microwave. It was shown that EGCG could interact with β-LG or U-β-LG to form β-LG-EGCG complex or U-β-LG-EGCG complex. The main binding force between EGCG and β-LG or U-β-LG was hydrophobic interaction. The binding distance between donor and acceptor at 298 K were 3.188 and 2.875 nm for β-LG-EGCG complex and U-β-LG-EGCG complex, respectively based on the F?rster’s theory of non-radiative energy transfer. The two- and three-dimensional structures of β-LG and U-β-LG were changed and their surface hydrophobicity was decreased slightly after being combined with EGCG. The binding affinity between U-β-LG and EGCG was stronger than that between β-LG and EGCG, which contributed to greater conformational change of U-β-LG.

Key words: β-lactoglobulin (β-LG), epigallocatechin gallate (EGCG), fluorescence spectroscopy, ultraviolet spectroscopy, circular dichroism spectroscopy

CLC Number:

TS201.2

FU Shanlin, ZHONG Junzhen, YAO Wenjun, QIN Fangfang, LIU Chengmei, LIU Wei. Interaction between Unfolded Bovine β-Lactoglobulin and Epigallocatechin Gallate[J]. FOOD SCIENCE, 2019, 40(4): 7-13.

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Interaction between Unfolded Bovine β-Lactoglobulin and Epigallocatechin Gallate

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