不同pH值环境下β-乳球蛋白与咖啡中3种主要多酚之间的相互作用
TS201.2; 利用多光谱学和分子对接技术,探究在不同pH值条件下,咖啡中的3种主要多酚(绿原酸、咖啡酸和阿魏酸)与牛乳中β-乳球蛋白间的非共价相互作用及对蛋白结构的影响.结果表明,在两种pH值环境下,3种咖啡多酚均通过静态猝灭有效地猝灭β-乳球蛋白的荧光,在pH 7.4、温度298 K时,绿原酸、咖啡酸和阿魏酸对β-乳球蛋白的猝灭常数(Ksv)分别为6.53×104、3.16×104 L/mol及3.09× 104 L/mol,结合位点数分别为1.20、1.02和1.14,能量转移效率分别为34.55％、24.56％和21.35％;pH 3.0、温度298 K时,Ksv分别为7.18×10...
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| Published in | 食品科学 Vol. 45; no. 19; pp. 26 - 40 |
|---|---|
| Main Authors | , , , |
| Format | Magazine Article |
| Language | Chinese |
| Published |
华中农业大学食品科学技术学院,湖北武汉 430070
15.10.2024
国家重要热带作物工程技术研究中心,海南海口 570000 中国热带农业科学院香料饮料研究所,海南万宁 571533%中国热带农业科学院香料饮料研究所,海南万宁 571533 海南省特色热带作物加工适宜性与品质控制重点实验室,海南万宁 571533 |
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| Online Access | Get full text |
| ISSN | 1002-6630 |
| DOI | 10.7506/spkx1002-6630-20231104-027 |
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| Abstract | TS201.2; 利用多光谱学和分子对接技术,探究在不同pH值条件下,咖啡中的3种主要多酚(绿原酸、咖啡酸和阿魏酸)与牛乳中β-乳球蛋白间的非共价相互作用及对蛋白结构的影响.结果表明,在两种pH值环境下,3种咖啡多酚均通过静态猝灭有效地猝灭β-乳球蛋白的荧光,在pH 7.4、温度298 K时,绿原酸、咖啡酸和阿魏酸对β-乳球蛋白的猝灭常数(Ksv)分别为6.53×104、3.16×104 L/mol及3.09× 104 L/mol,结合位点数分别为1.20、1.02和1.14,能量转移效率分别为34.55％、24.56％和21.35％;pH 3.0、温度298 K时,Ksv分别为7.18×104、5.24×104 L/mol及7.12×104 L/mol,结合位点数为1.28、1.18和1.25,能量转移效率分别提高至34.70％、30.42％和29.65％.在pH 7.4时,β-乳球蛋白α-螺旋含量降低,β-折叠含量增加;pH 3.0时,β-折叠含量增加,无规卷曲含量降低.分子对接结果表明,3种多酚主要通过氢键和范德华力以及疏水相互作用结合在β-乳球蛋白的疏水口袋.本研究初步揭示不同pH值条件下咖啡乳饮料中β-乳球蛋白和绿原酸、咖啡酸及阿魏酸间的相互作用机制. |
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| AbstractList | TS201.2; 利用多光谱学和分子对接技术,探究在不同pH值条件下,咖啡中的3种主要多酚(绿原酸、咖啡酸和阿魏酸)与牛乳中β-乳球蛋白间的非共价相互作用及对蛋白结构的影响.结果表明,在两种pH值环境下,3种咖啡多酚均通过静态猝灭有效地猝灭β-乳球蛋白的荧光,在pH 7.4、温度298 K时,绿原酸、咖啡酸和阿魏酸对β-乳球蛋白的猝灭常数(Ksv)分别为6.53×104、3.16×104 L/mol及3.09× 104 L/mol,结合位点数分别为1.20、1.02和1.14,能量转移效率分别为34.55％、24.56％和21.35％;pH 3.0、温度298 K时,Ksv分别为7.18×104、5.24×104 L/mol及7.12×104 L/mol,结合位点数为1.28、1.18和1.25,能量转移效率分别提高至34.70％、30.42％和29.65％.在pH 7.4时,β-乳球蛋白α-螺旋含量降低,β-折叠含量增加;pH 3.0时,β-折叠含量增加,无规卷曲含量降低.分子对接结果表明,3种多酚主要通过氢键和范德华力以及疏水相互作用结合在β-乳球蛋白的疏水口袋.本研究初步揭示不同pH值条件下咖啡乳饮料中β-乳球蛋白和绿原酸、咖啡酸及阿魏酸间的相互作用机制. |
| Abstract_FL | The purpose of this study was to explore the non-covalent interactions between three major polyphenols(chlorogenic acid,caffeic acid and ferulic acid)in coffee and β-lactoglobulin(β-LG)at different pH values and their effects on protein structure by multispectroscopic techniques and molecular docking.The results showed that all three coffee polyphenols statically quenched the fluorescence of β-lactoglobulin under two pH conditions.At pH 7.4 and 298 K,the quenching constants(Ksv of chlorogenic acid,caffeic acid and ferulic acid for β-lactoglobulin were 6.53 × 104,3.16 × 104 and 3.09 × 104 L/mol with 1.20,1.02 and 1.14 binding sites and energy transfer efficiency of 34.55％,24.56％and 21.35％,respectively.At pH 3.0 and 298 K,the Ksv were 7.18 × 104,5.24 × 104 and 7.12 × 104 L/mol with 1.28,1.18 and 1.25 binding sites and energy transfer efficiency of 34.70％,30.42％and 29.65％,respectively.The results of circular dichroism showed that the α-helix content of β-LG decreased and the β-sheet content increased at pH 7.4,and the β-sheet content increased and the random coil content decreased at pH 3.0.The results of molecular docking showed that the three polyphenols could bind to the hydrophobic pocket of β-lactoglobulin mainly through hydrogen bonds,van der Waals force and hydrophobic interaction.This study preliminarily revealed the interaction mechanism between β-lactoglobulin and chlorogenic acid,caffeic acid and ferulic acid in coffee milk beverage under different pH conditions. |
| Author | 胡荣锁 董文江 翟晓宇 于鑫欣 |
| AuthorAffiliation | 华中农业大学食品科学技术学院,湖北武汉 430070;中国热带农业科学院香料饮料研究所,海南万宁 571533%中国热带农业科学院香料饮料研究所,海南万宁 571533;海南省特色热带作物加工适宜性与品质控制重点实验室,海南万宁 571533;国家重要热带作物工程技术研究中心,海南海口 570000 |
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| Author_FL | HU Rongsuo DONG Wenjiang ZHAI Xiaoyu YU Xinxin |
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| Keywords | molecular docking non-covalent interaction multispectroscopic techniques β-lactoglobulin 非共价相互作用 多光谱技术 多酚 polyphenol β-乳球蛋白 分子对接 |
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| Publisher | 华中农业大学食品科学技术学院,湖北武汉 430070 国家重要热带作物工程技术研究中心,海南海口 570000 中国热带农业科学院香料饮料研究所,海南万宁 571533%中国热带农业科学院香料饮料研究所,海南万宁 571533 海南省特色热带作物加工适宜性与品质控制重点实验室,海南万宁 571533 |
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| Snippet | TS201.2; 利用多光谱学和分子对接技术,探究在不同pH值条件下,咖啡中的3种主要多酚(绿原酸、咖啡酸和阿魏酸)与牛乳中β-乳球蛋白间的非共价相互作用及对蛋白结构的影响.结果表明,在两种pH值环境下,3种咖啡多酚均通过静态猝灭有效地猝灭β-乳球蛋白的荧光,在pH 7.4、温度298... |
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| Title | 不同pH值环境下β-乳球蛋白与咖啡中3种主要多酚之间的相互作用 |
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