摘要
Journal of Food BiochemistryEarly View e14416 ORIGINAL ARTICLE Cross-linking effects of EGCG on myofibrillar protein from common carp (Cyprinus carpio) and the action mechanism Chong Tan, Chong Tan Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, PR ChinaSearch for more papers by this authorQian-Da Xu, Qian-Da Xu Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, PR ChinaSearch for more papers by this authorNan Chen, Nan Chen Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, PR ChinaSearch for more papers by this authorQiang He, Qiang He The Key Laboratory of Food Science and Technology of Sichuan Province of Education, Sichuan University, Chengdu, PR ChinaSearch for more papers by this authorQun Sun, Qun Sun The Key Laboratory of Food Science and Technology of Sichuan Province of Education, Sichuan University, Chengdu, PR ChinaSearch for more papers by this authorWei-Cai Zeng, Corresponding Author Wei-Cai Zeng weicaizeng@qq.com orcid.org/0000-0002-5819-4333 Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, PR China The Key Laboratory of Food Science and Technology of Sichuan Province of Education, Sichuan University, Chengdu, PR China Correspondence Wei-Cai Zeng, Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, Sichuan 610065, PR China. Email: weicaizeng@qq.comSearch for more papers by this author Chong Tan, Chong Tan Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, PR ChinaSearch for more papers by this authorQian-Da Xu, Qian-Da Xu Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, PR ChinaSearch for more papers by this authorNan Chen, Nan Chen Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, PR ChinaSearch for more papers by this authorQiang He, Qiang He The Key Laboratory of Food Science and Technology of Sichuan Province of Education, Sichuan University, Chengdu, PR ChinaSearch for more papers by this authorQun Sun, Qun Sun The Key Laboratory of Food Science and Technology of Sichuan Province of Education, Sichuan University, Chengdu, PR ChinaSearch for more papers by this authorWei-Cai Zeng, Corresponding Author Wei-Cai Zeng weicaizeng@qq.com orcid.org/0000-0002-5819-4333 Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, PR China The Key Laboratory of Food Science and Technology of Sichuan Province of Education, Sichuan University, Chengdu, PR China Correspondence Wei-Cai Zeng, Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, Sichuan 610065, PR China. Email: weicaizeng@qq.comSearch for more papers by this author First published: 15 September 2022 https://doi.org/10.1111/jfbc.14416Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract The cross-linking effects and action mechanism of epigallocatechin gallate (EGCG) on myofibrillar protein from common carp (Cyprinus carpio) were investigated. According to particle size, zeta potential, and atomic force microscopy, EGCG could cause the aggregation of myofibrillar protein, while hydrogen bonds and electrostatic interactions were the main molecular forces. With the measurement of Fourier transform infrared spectrum, surface hydrophobicity, fluorescence spectrum, circular dichroism spectrum, and molecular dynamics simulation, EGCG could make the spatial configuration of myofibrillar protein loose, enhance the exposure of amino acid residues, and further change its secondary and tertiary structures by forming intermolecular and intramolecular hydrogen bonds with myofibrillar protein. In addition, the gel properties of myofibrillar protein were improved by EGCG. All results suggested that EGCG had the cross-linking effects on myofibrillar protein in carp meat and could further improve its properties, which showed the potential to improve the qualities of fish meat in food industry. Practical applications Compared with other meat, fish meat is particularly easy to break and deteriorate during its processing and sales due to the short length and low cross-linking degree of fish myofibrillar protein, which shows some negative impacts on the quality of fish meat. In the present study, epigallocatechin gallate (EGCG) showed the significant cross-linking effects on carp myofibrillar protein and further improved its physicochemical properties. All results suggested that EGCG had the potential to increase the cross-linking degree of fish myofibrillar protein and improve its properties, so as to ameliorate the quality of fish meat during processing and storage. CONFLICT OF INTEREST The authors have declared no conflict of interest. Open Research DATA AVAILABILITY STATEMENT Data sharing is not applicable to this article as no new data were created or analyzed in this study. 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