食品科学2024，Vol.45Issue(11)：61-67,7.DOI:10.7506/spkx1002-6630-20231101-001
迷迭香酸共价偶联对β-乳球蛋白结构及性质的影响
Effect of Covalent Coupling with Rosmarinic Acid on the Structure and Properties of β-Lactoglobulin
摘要
Abstract
The present study aimed to investigate the effect of covalent coupling with the dietary polyphenol rosmarinic acid(RA)on the structure and properties of β-lactoglobulin(β-LG).β-LG-RA complexes were prepared using the free radical and alkaline methods.The structural changes of β-LG after coupling with RA were analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis(SDS-PAGE),Fourier transform infrared(FTIR)spectroscopy,ultraviolet(UV)absorption spectroscopy,fluorescence spectroscopy,and circular dichroism(CD)spectroscopy.The antioxidant activity of β-LG and its complexes with RA was assessed using the 1,1-diphenyl-2-picrylhydrazyl(DPPH)radical and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid(ABTS)radical cation scavenging methods.Furthermore,their binding capacity to serum-specific immunoglobulin G(IgG)were evaluated using enzyme-linked immunosorbent assay(ELISA).The results revealed that the secondary structure of β-LG transformed from α-helix to β-sheet and random coil after RA covalent conjugation.The protein underwent changes in its secondary and tertiary structures.Additionally,compared to β-LG,theβ-LG-RA covalent conjugates showed significantly enhanced antioxidant activity and reduced binding ability with serum specific IgG.In conclusion,covalent coupling with RA led to a significant improvement in the antioxidant activity of β-LG and a significant decrease in its binding capacity to serum-specific IgG by introducing phenolic hydroxyl groups.关键词
β-乳球蛋白/迷迭香酸/共价偶联/蛋白结构/蛋白性质Key words
β-lactoglobulin/rosmarinic acid/covalent conjugation/protein structure/protein properties分类
轻工纺织引用本文复制引用
杨庆,尚洁丽,曾浩龙,王璇霈,陈义杰,柳鑫,宫智勇,许琳..迷迭香酸共价偶联对β-乳球蛋白结构及性质的影响[J].食品科学,2024,45(11):61-67,7.基金项目
大宗粮油精深加工教育部重点实验室开放课题项目(NJZ2022009) （NJZ2022009）
