ASSESSING THE EFFECT OF THERMAL TREATMENT ON MEAT PROTEINS USING PROTEOMIC METHODS

Irina M Chernukha,Anastasiya G Akhremko

doi:10.21323/2414-438x-2019-4-3-4-6

Abstract

The results of studying the effect of various temperatures on the protein composition of minced meat from porcine m. longissimus dorsi by two-dimensional electrophoresis are presented. The most complete distribution of protein fractions was observed in fresh raw minced meat, and when it was exposed to negative temperature, there was a sharp decrease in protein components (carbonic anhydrase 3, αβ-crystallin), as well as a decrease in the staining intensity of protein spots of the main constitutive fractions (tropomyosin alpha 1, myosin light chain 1). In the case of heat treatment, structural muscle proteins were retained with some changes in high molecular weight fractions, namely, protein molecules degraded to compounds with a simpler structure. It was noted that fractions of tropomyosin β-chain, triosephosphate isomerase 1, myosin light chains 2 were not detected after minced meat was frozen, while tropomyosin alpha 1 was retained in all samples.

Highlights

It is known that introduction of processing technologies with different temperature variations is of crucial significance to meat technological characteristics [1,2]
If meat products are exposed to the reactive oxygen species, the oxidative stress is induced by proteins, which cause chemical destruction, changes in protein functionality, loss of essential amino acids and possibly product digestibility [8]
Two-dimensional (2D) electrophoregram of investigated minced meat presented in Figure 1 showed similar distribution of fractions that corresponded to the multi-module database «Proteomics of Muscular Organs» [13] regarding Sus scrofa

Summary

Introduction

It is known that introduction of processing technologies with different temperature variations is of crucial significance to meat technological characteristics [1,2]. The conditions of treatment, especially temperature, cause a cascade of chemical and physical changes that affect meat proteins. A range of used temperature conditions for meat processing and its following preparation leads to potentially different impacts on protein modification. Basic and aromatic amino acids are transformed into carbonyl, and thiol groups are replaced with formation of disulfide bridges, which cause polymerization and subsequent aggregation of proteins [9]. Oxidation of aromatic amino acids can lead to denaturation, polymerization, aggregation, fragmentation, changes in hydrophobicity, solubility, gel formation and emulsification, which affect the physico-chemical condition of proteins [10]. The main aim of the research was to understand how an impact of different temperatures (freezing and heat treatment) can cause biochemical changes in meat systems, which can affect food quality of meat proteins, using comparative analysis of two-dimensional maps

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Conclusion