儿茶素与糖基化-猪血红蛋白相互作用对复合物功能特性及结构的影响

doi:10.3964/j.issn.1000-0593(2023)11-3615-07

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摘要：猪血红蛋白（PHb）可以赋予和提升食品在制备、加工和贮藏过程中的品质，但因其黏度大、性质不稳定、且血腥味较重而不被人们所接受等因素，限制了其在食品中的应用。因此，改性是提升其经济效益及生物可利用度的一种重要手段。探究了儿茶素（Catechin）与糖基化猪血红蛋白（G-PHb）相互作用对复合物（CG-PHb）功能特性及结构变化的影响。以PHb和G-PHb为对照，研究CG-PHb的溶解度、浊度、乳化性能、表面疏水性以及抗氧化性等功能特性，采用紫外-可见光谱、荧光光谱、傅里叶变换红外光谱和扫描电镜，分析CG-PHb的结构变化。结果表明：相较于PHb和G-PHb，CG-PHb的溶解度显著提高（p<0.05），浊度显著降低（p<0.05）；乳化性以及乳化稳定性相较于对照组，分别提高了38.36%、21.31%和16.08%、3.69%（p<0.05）；三者中CG-PHb的表面疏水性最大；抗氧化性随着溶液浓度的升高不断增大，溶液浓度为1.60 g·mL^-1时，抗氧化性最高达93.60%；CG-PHb的紫外吸收峰相较于对照组峰形变宽、峰值增大且略微红移；荧光峰强度大小为：CG-PHb>PHb>G-PHb，且随着儿茶素的浓度增大，G-PHb的荧光猝灭效果呈现增强趋势，并发生红移现象；CG-PHb的酰胺I带向低波数方向移动，且二级结构含量中β-折叠含量显著增加（p<0.05），其余结构含量减少（p<0.05）；此外，电镜结果表明，由于糖基基团的嵌入及与儿茶素之间的作用力，使蛋白质的结构发生了变化，CG-PHb的表面孔洞结构增加，有利于其功能特性的发挥。该研究可以为蛋白质的改性研究提供新思路，为复合物在食品加工过程中的性质变化提供理论基础及参考。

关键词：糖基化；猪血红蛋白；儿茶素；相互作用；结构特性

Abstract：Porcine hemoglobin (PHb) can endow and improve food quality during preparation, processing and storage. However, it is limited to be used in food because of its high viscosity, unstable properties and heavy blood smell, which people do not accept. Therefore, modification is important to improve its economic benefits and bioavailability. This study investigated the effect of the interaction between catechin and glycosylated porcine hemoglobin (G-PHb) on the functional characteristics and structure of the complex of catechin and glycosylated porcine hemoglobin (CG-PHb). PHb and G-PHb were used as controls. The solubility, turbidity, emulsifying property, surface hydrophobicity and oxidation resistance of CG-PHb were studied.The structural changes of the CG-PHb were analyzed via UV-Vis, FS, FT-IR and SEM. The results show that the solubility of CG-PHB increased significantly (p<0.05), and the turbidity decreased significantly (p<0.05). The emulsifying activity and stability were increased by 38.36%, 21.31%, 16.08% and 3.69% respectively (p<0.05), compared with the control group. CG-PHB has the largest surface hydrophobicity among the PHb, G-PHb and CG-PHB. When the concentration of the solution was increased to 1.60 g·mL^-1, the oxidation resistance was enhanced to 93.60%. Compared with the PHb and G-PHb, the UV absorption peak of CG-PHb has a wider peak shape, a larger peak and a slight red shift. The fluorescence peak intensity is CG-PHb>PHb>G-PHb. The secondary structure of CG-PHb was changed. Its β-sheet content increased significantly (p<0.05), but the content of α-helix, β-turn and irregular curl decreased (p<0.05). In addition, the scanning electron microscope showed that the protein structure changed due to the embedding of glycosyl groups and the interaction between glycosyl groups and catechins. It leads to the increase of the surface pore structure of CG-PHB. It is conducive to the exertion of its functional characteristics. This study can provide new ideas for protein modification research and provide a theoretical basis and reference for the property changes of the compound during food processing.

Key words：Glycosylation; Porcine hemoglobin (PHb); Catechin; Interaction; Structural characteristics

收稿日期: 2022-04-26 修订日期: 2022-09-22

中图分类号:

TS251.93

基金资助: 2021年洛阳市社会发展专项（2101021A），国家自然科学基金项目（U1704114）资助

通讯作者: 刘丽莉 E-mail: yangliuyilang@126.com

作者简介: 郭净芳，女，1997年生，河南科技大学食品与生物工程学院硕士研究生 e-mail: guojingfang_2020@163.com

引用本文:

郭净芳，刘丽莉，程伟伟，徐宝成，张潇丹，于影. 儿茶素与糖基化-猪血红蛋白相互作用对复合物功能特性及结构的影响[J]. 光谱学与光谱分析, 2023, 43(11): 3615-3621.
GUO Jing-fang, LIU Li-li, CHENG Wei-wei, XU Bao-cheng, ZHANG Xiao-dan, YU Ying. Effect of Interaction Between Catechin and Glycosylated Porcine Hemoglobin on Its Structural and Functional Properties. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2023, 43(11): 3615-3621.

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