Zhao Xue, Xu Xinglian, Zhou Guanghong
Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control; Key Laboratory of Animal Products Processing, MOA; Key Lab of Meat Processing and Quality Control, MOE; College of Food Science and Technology, Nanjing Agricultural University, Nanjing, P.R. China.
Compr Rev Food Sci Food Saf. 2021 Jan;20(1):924-959. doi: 10.1111/1541-4337.12684. Epub 2020 Dec 19.
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.
提高肉制品质量一直是肉类行业和科学家们关注的焦点。作为肉类蛋白质的主要成分，肌原纤维蛋白（MPs）的凝胶化特性主要决定了最终产品的感官质量和产品产量。已知天然或人工发生的共价修饰会通过改变蛋白质结构和形成聚集体而在很大程度上影响MP的功能，从而产生有利和不利的结果。本综述旨在总结与几种共价修饰相关的机制以及增强MP凝胶化特性的最新进展。讨论了控制氧化、酚类-蛋白质相互作用、酶催化、糖基化以及等电溶解/沉淀的各种外在和内在参数，以及它们对热诱导MP凝胶特性的影响。本文增进了对主要发生在MP系统中的共价修饰以及如何利用它们来促进其凝胶化特性的理解。共价修饰对MP凝胶化特性表现出剂量依赖性和双重作用方式。温和的氧化、酶催化和等电溶解/沉淀处理有利于形成更有序和交联的MP凝胶三维网络，因为蛋白质聚集程度适中。然而，过度的聚集体会阻碍MP的凝胶化行为，导致凝胶化质量下降。糖基化有效地增加了MP的亲水性，酚类共轭赋予MP新的生物活性。合理利用这样一个过程甚至将它们合理组合，能够增强具有各种理想功能的MP的凝胶化特性，并进一步提高肉制品的质量。
