{"title":"综合多光谱和分子动力学模拟探索酚类化合物与海鲈肌纤维蛋白的相互作用机理","authors":"Yujie Zhu, Mingyu Li, Rongbin Zhong, Feifei Shi, Qian Yang, Peng Liang","doi":"10.1007/s11947-024-03372-6","DOIUrl":null,"url":null,"abstract":"<p>Polyphenol compounds can modify myofibrillar proteins to improve the quality of fish and surimi. Nevertheless, research into the precise mechanisms of interaction between phenolic substances and sea bass myofibrillar proteins is lacking. This study aimed to explore the interaction mechanism between five phenolic compounds (caffeic acid (CFA), gallic acid (GA), chlorogenic acid (CHA), resveratrol (RES), and catechin (CAT)) with sea bass myofibrillar protein (MP). The results of UV–vis absorption spectroscopy, Fourier transform infrared (FT-IR) spectroscopy, and fluorescence spectroscopy (namely, multi-spectroscopy) showed that all five phenolic compounds could spontaneously form new complexes with MP, with a binding molar ratio of 1:1. The interaction between CFA and MP is predominantly electrostatic, while the interaction between GA and MP is mainly hydrophobic. The rest of phenolic compounds and MP are mediated by hydrogen bonds and van der Waals forces. And molecular dynamics (MD) simulations indicated that CHA-myosin had the minimum root mean square deviation, while CFA-myosin had the smallest Rg value. In addition, the amino acid Lys-179 was the key residue for the interaction between five phenolic compounds and myosin. This study contributes to a better understanding of the interaction between phenolic compounds and sea bass MP, which could develop the processing of aquatic food products.</p>","PeriodicalId":562,"journal":{"name":"Food and Bioprocess Technology","volume":null,"pages":null},"PeriodicalIF":5.3000,"publicationDate":"2024-04-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Integrated Multi-Spectroscopy and Molecular Dynamics Simulations to Explore the Interaction Mechanism of Phenolic Compounds and Sea Bass Myofibrillar Protein\",\"authors\":\"Yujie Zhu, Mingyu Li, Rongbin Zhong, Feifei Shi, Qian Yang, Peng Liang\",\"doi\":\"10.1007/s11947-024-03372-6\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p>Polyphenol compounds can modify myofibrillar proteins to improve the quality of fish and surimi. Nevertheless, research into the precise mechanisms of interaction between phenolic substances and sea bass myofibrillar proteins is lacking. This study aimed to explore the interaction mechanism between five phenolic compounds (caffeic acid (CFA), gallic acid (GA), chlorogenic acid (CHA), resveratrol (RES), and catechin (CAT)) with sea bass myofibrillar protein (MP). The results of UV–vis absorption spectroscopy, Fourier transform infrared (FT-IR) spectroscopy, and fluorescence spectroscopy (namely, multi-spectroscopy) showed that all five phenolic compounds could spontaneously form new complexes with MP, with a binding molar ratio of 1:1. The interaction between CFA and MP is predominantly electrostatic, while the interaction between GA and MP is mainly hydrophobic. The rest of phenolic compounds and MP are mediated by hydrogen bonds and van der Waals forces. And molecular dynamics (MD) simulations indicated that CHA-myosin had the minimum root mean square deviation, while CFA-myosin had the smallest Rg value. In addition, the amino acid Lys-179 was the key residue for the interaction between five phenolic compounds and myosin. This study contributes to a better understanding of the interaction between phenolic compounds and sea bass MP, which could develop the processing of aquatic food products.</p>\",\"PeriodicalId\":562,\"journal\":{\"name\":\"Food and Bioprocess Technology\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":5.3000,\"publicationDate\":\"2024-04-23\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food and Bioprocess Technology\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://doi.org/10.1007/s11947-024-03372-6\",\"RegionNum\":2,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"FOOD SCIENCE & TECHNOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food and Bioprocess Technology","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1007/s11947-024-03372-6","RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
Integrated Multi-Spectroscopy and Molecular Dynamics Simulations to Explore the Interaction Mechanism of Phenolic Compounds and Sea Bass Myofibrillar Protein
Polyphenol compounds can modify myofibrillar proteins to improve the quality of fish and surimi. Nevertheless, research into the precise mechanisms of interaction between phenolic substances and sea bass myofibrillar proteins is lacking. This study aimed to explore the interaction mechanism between five phenolic compounds (caffeic acid (CFA), gallic acid (GA), chlorogenic acid (CHA), resveratrol (RES), and catechin (CAT)) with sea bass myofibrillar protein (MP). The results of UV–vis absorption spectroscopy, Fourier transform infrared (FT-IR) spectroscopy, and fluorescence spectroscopy (namely, multi-spectroscopy) showed that all five phenolic compounds could spontaneously form new complexes with MP, with a binding molar ratio of 1:1. The interaction between CFA and MP is predominantly electrostatic, while the interaction between GA and MP is mainly hydrophobic. The rest of phenolic compounds and MP are mediated by hydrogen bonds and van der Waals forces. And molecular dynamics (MD) simulations indicated that CHA-myosin had the minimum root mean square deviation, while CFA-myosin had the smallest Rg value. In addition, the amino acid Lys-179 was the key residue for the interaction between five phenolic compounds and myosin. This study contributes to a better understanding of the interaction between phenolic compounds and sea bass MP, which could develop the processing of aquatic food products.
期刊介绍:
Food and Bioprocess Technology provides an effective and timely platform for cutting-edge high quality original papers in the engineering and science of all types of food processing technologies, from the original food supply source to the consumer’s dinner table. It aims to be a leading international journal for the multidisciplinary agri-food research community.
The journal focuses especially on experimental or theoretical research findings that have the potential for helping the agri-food industry to improve process efficiency, enhance product quality and, extend shelf-life of fresh and processed agri-food products. The editors present critical reviews on new perspectives to established processes, innovative and emerging technologies, and trends and future research in food and bioproducts processing. The journal also publishes short communications for rapidly disseminating preliminary results, letters to the Editor on recent developments and controversy, and book reviews.