牛血清白蛋白与槲皮素及花青素相互作用方式及其纳米颗粒特征的比较

发布时间：2018-01-28 13:11

本文关键词： 牛血清白蛋白槲皮素花青素相互作用纳米颗粒　出处：《食品科学》2017年05期 　论文类型：期刊论文

【摘要】：实验比较了牛血清白蛋白(bovine serum albumin,BSA)与脂溶性小分子槲皮素(quercetin,QUE)和水溶性花青素(anthocyanin,ACN)相互作用方式及其纳米颗粒的特征。QUE对BSA荧光猝灭作用为静态猝灭方式(低浓度),但在较高浓度时为静态与动态并存的复合猝灭方式,两者的相互作用力为疏水作用力;ACN对BSA的荧光猝灭程度小于QUE对BSA的,为静态猝灭方式,相互作用力为静电作用力。BSA与QUE的结合常数大于BSA与ACN的结合常数。BSA与QUE或ACN相互作用可形成纳米颗粒,其大小分别为42.5 nm和53.7 nm,ζ-电势分别为-25.64 m V和-21.50 m V。1 mol BSA分子可分别与8 mol QUE和10 mol ACN结合。BSA与QUE形成的纳米颗粒(BSA-QUE)粒径较BSA与ACN(BSA-ACN)的小,且稳定性较高。BSA-QUE对DPPH自由基和ABTS+·清除率均高于BSA-ACN。
[Abstract]:Bovine serum albumin (BSA) and fat-soluble small molecule quercetin were compared. The interaction mode between que and water-soluble anthocyanin ACNand the characteristics of nanoparticles. The fluorescence quenching of BSA by que was static quenching mode (low concentration). But at higher concentration, there is a compound quenching mode of static and dynamic coexistence, and the interaction force of the two is hydrophobic force. The fluorescence quenching degree of BSA by ACN is less than that of BSA by QUE, which is a static quenching mode. The interaction force is electrostatic force. The binding constant of BSA and QUE is larger than that of BSA and ACN. BSA interacts with QUE or ACN to form nanoparticles. Their sizes are 42.5 nm and 53.7 nm, respectively. 味-potential of -25.64 MV and -21.50 MV of 1 mol BSA molecule can be compared with 8 mol QUE and 10 mol, respectively. Nanocrystalline particles formed by ACN binding. BSA and QUE (. The particle size of BSA-QUEwas smaller than that of BSA and ACN-BSA-ACN. The stability of BSA-QUE on DPPH free radical and ABTS 路scavenging rate was higher than that of BSA-ACN.
【作者单位】：中国农业大学食品科学与营养工程学院;
【基金】：国家自然科学基金面上项目(31171676)
【分类号】：Q50;TB383.1
【正文快照】： 牛血清白蛋白(bovine serum albumin,BSA)是牛中溶解性较好,容易纯化,具有较好的小分子物质结合血清中最主要的蛋白质,其来源丰富,价格便宜,在水特性[1]。BSA是单链蛋白质,由583个氨基酸残基组成, 含3个结构相似的结构域(domainⅠ、Ⅱ、Ⅲ),每美国Amresco公司;QUE(色谱级,纯

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