Myofibrillar Protein Cross-Linking and Gelling Behavior Modified by Structurally Relevant Phenolic Compounds

Area of Science:

• Food Science
• Protein Chemistry
• Food Chemistry

Background:

• Protein gelation is crucial for the texture and quality of processed meats.
• Phenolic compounds are known for their antioxidant properties and potential to modify food matrices.

Purpose of the Study:

• To investigate the structure-activity relationship of six phenolic compounds in a myofibrillar protein (MP) gelling system.
• To evaluate the impact of these phenolics on MP gelation and lipid oxidation under oxidative conditions.

Main Methods:

• Assessed the effect of gallic acid (GA), chlorogenic acid (CA), propyl gallate (PG), quercetin (QT), catechin (CC), and (-)-epigallocatechin-3-gallate (EGCG) on MP unfolding and cross-linking.
• Measured MP gel strength and elasticity.
• Evaluated lipid oxidation in MP-emulsion composite gels during refrigerated storage.

Main Results:

• All tested phenolics induced MP unfolding and cross-linking via sulfhydryl or amine groups.
• Propyl gallate (PG) and quercetin (QT) significantly enhanced MP gel strength.
• Phenolics, particularly PG and QT, effectively retarded lipid oxidation in MP-emulsion composite gels.

Conclusions:

• The structure of phenolic compounds influences their efficacy in modifying protein gelation and antioxidant activity.
• Phenolics offer a promising approach to improve the quality and stability of processed meat products.