没食子酸与猪血红蛋白的相互作用及对其稳定性的影响  

Interaction of Gallic Acid with Porcine Hemoglobin and Effect on the Stability

作　　者：周垚卿 董静雯 何强[1] ZHOU Yaoqing;DONG Jingwen;HE Qiang(College of Biomass Science and Engineering,Sichuan University,Chengdu 610065,C hina)

机构地区：[1]四川大学轻工科学与工程学院,四川成都610065

出　　处：《食品科技》2020年第2期117-121,共5页Food Science and Technology

基　　金：中央其他部委项目(2018-QT-工信部节函(2017)327号-105)。

摘　　要：猪血红蛋白(Porcine hemoglobin,PHb)的结构在一定理化因素(温度、pH)条件下稳定性较差,可能会出现亚铁血红素损失及蛋白质变性等现象。没食子酸(Gallic acid,GA)作为一种天然抗氧化剂,与PHb作用能影响PHb的结构稳定性。文章探讨了不同温度、pH条件下添加GA对PHb结构稳定性的影响,采用荧光光谱法研究了GA和PHb在模拟生理条件下的作用机制。结果表明,GA能一定程度提高PHb的热稳定性和酸稳定性。GA对PHb的内源荧光的淬灭方式为动态淬灭,298 K下的结合常数为0.70/104 M-1,PHb上仅有一个GA结合位点。疏水相互作用为GA与PHb之间的主要作用力,两者之间反应可自发进行。该研究可为GA在肉制品中的应用提供理论依据。The structure of porcine hemoglobin (PHb) is not stable under physical and chemical factors (temperature and pH).It may cause heme loss and protein denaturation.As a natural antioxidant,gallic acid (GA) could affect the structure stability of PHb by interaction with PHb.In this paper,the effects of adding GA at different temperatures and pH on the structure stability of PHb were studied.The mechanism of interaction of GA and PHb under simulated physiological conditions was studied by fluorescence spectroscopy.The results show that GA could improve the thermal stability and acid stability of PHb to a certain extent.The intrinsic fluorescence quenching mode is dynamic quenching.The binding constant at 298 K is 0.70/104 M-1.There is only one GA binding site on PHb.Hydrophobic interaction is the main force between GA and PHb,and the reaction between them can proceed spontaneously.This study can provide a theoretical basis for the application of GA in meat products.

关 键 词：猪血红蛋白 没食子酸 荧光光谱法 相互作用 稳定性 

分 类 号：TS251.1[轻工技术与工程—农产品加工及贮藏工程]