Cross‐linking effects of EGCG on myofibrillar protein from common carp ( Cyprinus carpio ) and the action mechanism

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.

Highly Effective Nobiletin–MPN in Yeast Microcapsules for Targeted Modulation of Oxidative Stress, NLRP3 Inflammasome Activation, and Immune Responses in Ulcerative Colitis

“…Subsequently, the intermolecular force in NEFY was analyzed by an FTIR spectrometer. Figure H shows that the characteristic absorption peak of YM at 3375 cm –1 corresponding to the O–H stretching vibration was red-shifted after the addition of NEF, which may be due to the introduction of O–H in EGCG at 3600–3375 cm –1 . In addition, the amide I band of YM at 1625 cm –1 was weakened, which may be due to the hydrogen bonding between protein N–H in YM and a large number of phenolic hydroxyl groups in EGCG .…”

Interactions between tea polyphenols and nutrients in food

“…Fish MP is short in length and possesses low cross‐linking, making it easily broken during processing. Similarly, TPs can strengthen the intermolecular and intramolecular forces of fish MP by hydrogen bonding, effectively increasing the degree of MP cross‐linking and improving its gel properties (Tan et al., 2022). However, high concentrations of TPs can severely deteriorate MP gelation, which may be caused by the exposure to hydrophobic domains of the proteins (Jia, Wang, et al., 2017).…”

Molecular simulation for food protein–ligand interactions: A comprehensive review on principles, current applications, and emerging trends

“…The results indicated that the secondary structure of hemoglobin did not change, whereas the antioxidant activity of hemoglobin improved due to the addition of piperine (Hu et al, 2022). Tan et al (2022) employed molecular dynamics simulation to prove that epigallocatechin-3gallate resulted in changing the spatial configuration of myofibrillar protein to the state of being loose, increasing the binding site for H-bonds to form. It improved the properties of the flesh of fish.…”

“…Tan et al. (2022) employed molecular dynamics simulation to prove that epigallocatechin‐3‐gallate resulted in changing the spatial configuration of myofibrillar protein to the state of being loose, increasing the binding site for H‐bonds to form. It improved the properties of the flesh of fish.…”

“…It improved the properties of the flesh of fish. In that case, it was suggested to add epigallocatechin‐3‐gallate to myofibrillar protein (Tan et al., 2022).…”