Changes in the Quality of Myofibrillar Protein Gel Damaged by High Doses of Epigallocatechin-3-Gallate as Affected by the Addition of Amylopectin.

Abstract

This work investigated the improvement of amylopectin addition on the quality of myofibrillar proteins (MP) gel damaged by high doses of epigallocatechin-3-gallate (EGCG, 80 μM/g protein). The results found that the addition of amylopectin partially alleviated the unfolding of MP induced by oxidation and EGCG, and enhanced the structural stability of MP. Amylopectin blocked the loss of the free amine group and thiol group, and increased the solubility of MP from 7.0% to 9.5%. The carbonyl analysis demonstrated that amylopectin addition did not weaken the antioxidative capacity of EGCG. It was worth noting that amylopectin significantly improved the gel properties of MP treated with a high dose of EGCG. The cooking loss was reduced from 51.2% to 35.5%, and the gel strength was reduced from 0.41 N to 0.29 N after adding high concentrations of amylopectin (A:E(8:1)). This was due to that amylopectin filled the network of MP gel after absorbing water and changed into a swelling state, and partially reduced interactions between EGCG and oxidized MP. This study indicated that amylopectin could be used to increase the polyphenol loads to provide a more lasting antioxidant effect for meat products and improve the deterioration of gel quality caused by oxidation and high doses of EGCG.