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Binding affinity, antioxidative capacity and in vitro digestion of complexes of grape seed procyanidins and pork, chicken and fish protein.
Food Research International ( IF 7.0 ) Pub Date : 2020-07-13 , DOI: 10.1016/j.foodres.2020.109530
Jingli Cong 1 , Jiemei Cui 1 , Haihui Zhang 1 , Courage Sedem Dzah 1 , Yuanqing He 1 , Yuqing Duan 2
Affiliation  

Studies have reported that procyanidins can interact with proteins, thereby affecting their structure, function, and bioaccessibility. In this paper, we investigated the interaction between grape seeds procyanidins (GSP) and animal source protein (from pig, chicken and fish), and the effects on the protein structure, antioxidant capacity and bioaccessibility of GSP. Fluorescence results showed that the binding constant of GSP-protein complex was 10-104 M-1, and the main forces were van der Waals force, hydrogen bonds and hydrophobic interactions. The antioxidant capacity of GSP was masked by GSP-protein complexes formed. The circular dichroism indicated that GSP had an effect on the content of α-helix and β-sheet in the secondary structure of pork and chicken proteins, but had little effect on the secondary structure of fish protein. The results showed that the protein can bind to GSP and affect its antioxidant activity and bioaccessibility. This study can provide reference for further study on the digestion and absorption of the complexes and offer health guidance in the preparation of diets.



中文翻译:

葡萄籽原花青素与猪肉,鸡肉和鱼类蛋白的复合物的结合亲和力,抗氧化能力和体外消化。

研究报道原花青素可以与蛋白质相互作用,从而影响其结构,功能和生物可及性。在本文中,我们研究了葡萄籽原花青素(GSP)与动物源蛋白(来自猪,鸡和鱼)之间的相互作用,以及其对蛋白结构,抗氧化能力和生物利用度的影响。荧光结果表明,GSP-蛋白复合物的结合常数为10-10 4 M -1,主要作用力是范德华力,氢键和疏水相互作用。GSP的抗氧化能力被形成的GSP-蛋白质复合物所掩盖。圆二色性表明,GSP对猪肉和鸡肉蛋白质二级结构中α-螺旋和β-折叠的含量有影响,而对鱼类蛋白质二级结构的影响很小。结果表明该蛋白可以与GSP结合并影响其抗氧化活性和生物可及性。该研究可为进一步研究复合物的消化吸收提供参考,并为饮食准备提供健康指导。

更新日期:2020-07-13
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