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枸杞叶黄酮与不同蛋白质的相互作用及体外抗氧化活性比较
方甜,廖家乐,范艳丽,王方舟
0
(宁夏大学食品与葡萄酒学院,银川750021;宁夏华宝枸杞产业有限责任公司,中宁755100; 宁夏回族自治区枸杞生物发酵与制粉工程技术研究中心,中宁755100)
摘要:
采用自由基诱导法制备蛋白质—枸杞叶黄酮复合物,通过紫外光谱、荧光光谱、傅里叶变换红外光谱、电镜等方法表征5种蛋白质(醇溶蛋白、大豆蛋白、酪蛋白、牛血清蛋白和乳清蛋白)与枸杞叶黄酮共价结合前后蛋白质结构的变化并进行了抗氧化性的分析。结果表明,5种蛋白质都与枸杞叶黄酮发生了不同程度地相互作用,并使蛋白质的结构发生改变。枸杞叶黄酮与蛋白质共价结合,导致蛋白质荧光淬灭,改变了酪氨酸或色氨酸数量。傅里叶变换红外光谱中酰胺A带、Ⅰ带、Ⅱ带的特征峰发生偏移,表明蛋白质在共价复合枸杞叶黄酮后二级结构发生了改变。扫描电镜直观显示了共价复合物微观结构的变化,可形成球状、片状、棒状或不规则颗粒状。综合比较发现,醇溶蛋白、乳清蛋白与枸杞叶黄酮结合能力较强,对蛋白质的二级结构影响较大,且体外抗氧化活性较强。研究结果为进一步分析枸杞叶黄酮与蛋白质共价复合物的性质以及枸杞叶黄酮类化合物作为天然抗氧化剂的应用提供理论基础。
关键词:  枸杞叶黄酮  蛋白质  相互作用  抗氧化
DOI:10.13610/j.cnki.1672-352x.20220325.012
基金项目:宁夏重点研发项目(2020BBF03014)和宁夏回族自治区柔性引进团队项目(KJT201701)共同资助。
Interaction of flavonoids from Lycium barbarum leaves with different proteins and comparison of antioxidant activity in vitro
FANG Tian,LIAO Jiale,FAN Yanli,WANG Fangzhou
(School of Food & Wine, Ningxia University, Yinchuan 750021;Ningxia Red Power Goji Co., LTD., Zhongning 755100; Ningxia Engineering Research Center for Goji Biological Fermentation & Milling, Zhongning 755100)
Abstract:
The complexes of proteins and flavonoids from Lycium barbarum leaves (LBLF) were prepared by the free radical induction method, and the protein structure changes of five kinds of protein (prolamin, soybean protein, casein, bovine serum protein and whey protein) binding covalently with LBLF before and after were characterized by ultraviolet spectrum, fluorescence spectrum, Fourier transform infrared spectroscopy, electric mirror and other methods and the antioxidant properties were analyzed. The results showed that the five kinds of protein all interacted with LBLF in different degrees and changed the protein structure. The covalent bonding between LBLF and protein resulted in quenching of protein fluorescence and changed the amount of tyrosine or tryptophan. The characteristic peaks of amide A band, band I, and band II in the Fourier transform infrared spectroscopy were shifted, which indicated that the secondary structure of the protein was changed after covalently binding with LBLF. Scanning electron microscopy visually showed the changes in the microstructure of the covalent complexes, which can form spherical, flake, rod or irregular granular shapes. Comprehensive comparison found that: prolamin and whey protein have a strong binding capacity with LBLF, a greater impact on the secondary structure of protein and a strong in vitro antioxidant activity. The results can provide a theoretical basis for further analysis of the properties of LBLF, protein covalent complex and the application of LBLF as natural antioxidants.
Key words:  flavonoids from Lycium barbarum leaves  protein  interaction  antioxidation

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