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紫苏籽粕蛋白与不同多酚之间的共轭相互作用对蛋白质结构和功能特性的影响。

Effects of conjugated interactions between Perilla seed meal proteins and different polyphenols on the structural and functional properties of proteins.

作者信息

Wang Dan, Li He, Hou Tian-Yu, Zhang Zhi-Jun, Li Hui-Zhen

机构信息

School of Chemistry and Chemical Engineering, North University of China, Taiyuan 030051, China.

School of Chemistry and Chemical Engineering, North University of China, Taiyuan 030051, China.

出版信息

Food Chem. 2024 Feb 1;433:137345. doi: 10.1016/j.foodchem.2023.137345. Epub 2023 Aug 30.

DOI:10.1016/j.foodchem.2023.137345
PMID:37666124
Abstract

The study aims to perform alkali-induced covalent modification of perilla seed meal protein (PSMP) using different polyphenols: gallic acid (GA), protocatechuic acid (PCA), caffeic acid (CA), apigenin (API) and luteolin (LU). Covalent binding between different polyphenols and PSMP was found to occur, with PSMP-LU showing the highest binding rate of 90.89 ± 1.37 mg/g; the fluorescence spectrum of PSMP-CA showed a maximum blue shift of Δ13.4 nm; the solubility increased from 69.626 ± 1.39 % to 83.102 ± 0.98 %. In order to better understand how these covalent conjugates, stabilize -carotene in emulsions, they were utilized as emulsifiers in an emulsion delivery method. The work further reveals the formation of PSMP-polyphenol conjugates and develops a novel emulsification system to deliver readily decomposable functional factors, providing a potential scenario for the application of PSMP and bioactive conjugates.

摘要

该研究旨在使用不同的多酚类物质

没食子酸(GA)、原儿茶酸(PCA)、咖啡酸(CA)、芹菜素(API)和木犀草素(LU)对紫苏籽粕蛋白(PSMP)进行碱诱导的共价修饰。研究发现不同多酚类物质与PSMP之间会发生共价结合,其中PSMP-LU的结合率最高,为90.89±1.37mg/g;PSMP-CA的荧光光谱最大蓝移为Δ13.4nm;溶解度从69.626±1.39%增加到83.102±0.98%。为了更好地理解这些共价缀合物如何在乳液中稳定β-胡萝卜素,将它们用作乳液递送方法中的乳化剂。这项工作进一步揭示了PSMP-多酚缀合物的形成,并开发了一种新型乳化系统来递送易分解的功能因子,为PSMP和生物活性缀合物的应用提供了一种潜在方案。

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