Covalent chemical modification of myofibrillar proteins to improve their gelation properties: A systematic review

Abstract

To improve the quality of meat products is a constant focus for both the meat industry and scientists. As major components in meat protein, the gelation properties of myofibrillar proteins (MPs) predominantly determine the sensory quality and product yield of the final product. Naturally or artificially occurring covalent modifications are known to largely affect MP functionality by changing the protein structure and forming aggregates, leading to both favorable and unfavorable outcomes. The review aims to summarize the mechanisms associated with several covalent modifications and the recent developments in enhancing MP gelation properties. Various extrinsic and intrinsic parameters controlling oxidation, phenolic–protein interactions, enzyme catalysis, glycation, and isoelectric solubilization/precipitation, and their effects on the characteristics of heat‐induced MP gels are discussed. This article provides an improved understanding of the covalent modifications that occur mainly in the MP system and how they can be utilized to promote its gelation properties. Covalent modifications exhibited dose‐dependent and dual‐role manners for MP gelation properties. Mild oxidation, enzyme catalysis, and isoelectric solubilization/precipitation treatment would be beneficial to form more aligned and cross‐linked three‐dimensional networks for MP gels because of moderate protein aggregation. However, an excessive aggregate impedes the MP gelation behavior, leading to reduced gelation quality. Glycation effectively increased hydrophilicity of MPs and phenolic conjugation provides MPs with novel bioactivity. A proper utilization of such a process or even a rational combination of them allowed us to enhance the gelation properties of MP with assorted appreciated functionalities and further improve the quality of meat products.

Ultrasound-assisted covalent reaction of myofibrillar protein: The improvement of functional properties and its potential mechanism

“…Interestingly, SSA of the MP was higher with the ultrasound-assisted oxidation system of ECG, compared to BN. This clearly evidenced that ECG is prone to be oxidized since the dispersion of hydrophilic polyphenol is better at this time [7] , [11] . Besides, more benzene rings and phenolic hydroxyl groups in ECG give MP more flexible structure through non-covalent force [9] , [38] , leading to the significant increase of SSA under cavitation.…”

“…This may be related to the chemical structure of these two polyphenols. More benzene rings and phenolic hydroxyl groups in ECG promote the non-covalent interaction between MP and polyphenols and indirectly restrict the expansion of protein structure [7] , [9] . Meanwhile, the sensitivity of MP after ultrasound was enhanced [19] , [45] , thereby promoting the exposure of –SH under the action of nonpolar polyphenols.…”

“…However, modern industrial applications of MPs are often compromised by their inherent imperfect nature, such as relative aggregation state and poor functionality [6] . These shortcomings could be alleviated by different structural modifications including physical and chemical ways [7] . Thereinto, chemical modification is the most conventional method to introduce functional groups into MPs, resulting in the transformation of structure and functional properties in protein [8] .…”

“…In addition, hydrogen peroxide is challenging to be avoided in free radical grafting method. For this reason, the industrial application of this reagent may be significantly restricted on account of its strong oxidation abilities [7] . In comparison, the alkaline reaction may be a suitable option, but its oxidative effect is usually undesirable, even ineffective [4] .…”

Pistachio Hull Extract as a Practical Strategy to Extend the Shelf Life of Raw Minced Beef: Chemometrics in Quality Evaluation

“…Similarly, the decline in carbonyl groups was previously disclosed using beef patties [33], beef meat balls [34], and minced beef meat [7,8,13]. us, protein degradation, denaturation, and loss of functionality are due to the formation of protein carbonyls from amino acid side chains caused by the impairment of myofibrillar protein conformation [35].…”