Volume 46, Issue 12 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 China

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Qian-Da Xu

Qian-Da Xu

Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, PR China

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Nan Chen

Nan Chen

Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, PR China

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Qiang He

Qiang He

The Key Laboratory of Food Science and Technology of Sichuan Province of Education, Sichuan University, Chengdu, PR China

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Qun Sun

Qun Sun

The Key Laboratory of Food Science and Technology of Sichuan Province of Education, Sichuan University, Chengdu, PR China

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Wei-Cai Zeng

Corresponding Author

Wei-Cai Zeng

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: [email protected]

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First published: 15 September 2022
Citations: 17

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.

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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