2种黑豆球蛋白与矢车菊素-3-O-葡萄糖苷的相互作用研究  

Study on Interaction Between Two Black Bean Globulins and Cyanidin-3-O-Glucoside

作　　者：刘金杰 马梦瑶 谢岩黎[1] 杨玉辉 孙淑敏[1] 马卫宾 李倩 LIU Jinjie;MA Mengyao;XIE Yanli;YANG Yuhui;SUN Shumin;MA Weibin;LI Qian(College of Food Science and Engineering/Henan Key Laboratory of Cereal and Oil Food Safety Inspection and Control,Henan University of Technology,Zhengzhou 450001,China)

机构地区：[1]河南工业大学粮油食品学院/河南省粮油食品安全检验与控制重点实验室,河南郑州450001

出　　处：《食品科学技术学报》2024年第4期101-113,共13页Journal of Food Science and Technology

基　　金：国家自然科学基金资助项目(31972003);河南省高校科技创新团队项目(20IRTSTHN023)。

摘　　要：矢车菊素-3-O-葡萄糖苷(cyanidin-3-O-glucoside,C3G)在不同pH值环境中的主要存在形式不同,其抗氧化能力也有所差异。黑豆蛋白是一种常见的膳食蛋白,具有作为不稳定生物活性化合物载体的潜力,了解黑豆球蛋白与C3G的相互作用机制有利于它们在食品体系中的应用。通过多种光谱学分析和分子对接实验研究了pH值为2.0、5.0和7.0时黑豆β-伴大豆球蛋白(7S)和大豆球蛋白(11S)与C3G的相互作用及其对C3G氧化稳定性和抗氧化能力的影响。研究结果表明,pH值为2.0和5.0时,C3G与7S和11S结合不仅导致Tyr残基周围的疏水环境减少,极性增加,而且使7S和11S中α-螺旋增加,β-折叠比例下降。pH值为7.0时,C3G的存在使7S和11S中α-螺旋和β-折叠的占比呈增加趋势,但β-转角比例降低。此外,C3G与7S和11S结合是一个放热过程,在不同pH值条件下,C3G与7S和11S主要通过氢键和范德华力相互作用使7S和11S静态荧光猝灭。7S和11S均在pH值为7.0时对C3G亲和力最强。分子对接结果表明,7S上的GLU229、ARG356和PRO101残基,11S上的ARG161、VAL162、ILE171和THR176残基在与C3G结合中起关键作用。在不同pH值条件下,7S、11S与C3G结合后均显著增强了C3G的氧化稳定性和抗氧化能力。The main forms of cyanidin-3-O-glucoside(C3G)in various pH environments are different,leading to differences in its antioxidant capacity.Black bean protein,a common dietary protein,has the potential to serve as a carrier for unstable bioactive compounds.Understanding the interaction mechanism between black bean protein and C3G is beneficial for their application in food systems.Interactions between β-conglycinin(7S)and glycinin(11S)soybean proteins with C3G and their effects on the oxidative stability and antioxidant capacity of C3G at pH 2.0,5.0,and 7.0 were investigated using various spectroscopic analyses and molecular docking experiments.The results showed that binding of C3G with 7S and 11S at pH 2.0 and 5.0 not only reduced the hydrophobic environment around Tyr residues and increased polarity,but also increasedα-helical content and decreasedβ-sheet content in both 7S and 11S.At pH 7.0,the presence of C3G led to an increase in bothα-helical andβ-sheet content in 7S and 11S except forβ-turns.Furthermore,the binding of C3G with 7S and 11S was an exothermic process,and at different pH conditions,hydrogen bonding and van der Waals forces were the main driving forces for the interaction between C3G with 7S and 11S,resulting in static fluorescence quenching of 7S and 11S.Both 7S and 11S exhibited the highest affinity for C3G at pH 7.0.Molecular docking revealed that GLU229,ARG356,and PRO101 residues on 7S,and ARG161,VAL162,ILE171,and THR176 residues on 11S played key roles in the binding with C3G.Moreover,the binding of 7S and 11S with C3G significantly enhanced the oxidative stability and antioxidant capacity of C3G at different pH conditions.

关 键 词：矢车菊素-3-O-葡萄糖苷 Β-伴大豆球蛋白 大豆球蛋白 相互作用 光谱特征 分子模拟 

分 类 号：TS214.2[轻工技术与工程—粮食、油脂及植物蛋白工程]