Abstract
The effect of animal and plant proteases as well as starters, or starter cultures, on protein aggregates for- mation in raw pork and beef as well as meat products was studied. The proteomic analysis of raw meat revealed that animal proteases – pepsin and trypsin – caused the aggregation of isoform 2 of protein 1 containing 4.5 LIM domains. Vacuum packaged meat showed the same results during storage, while unpacking led to the acceleration of the aggregation process due to autolysis. In addition, mixed aggregated fragments, such as muscle creatine phos- phokinase and glutathione-S-transferase, actin and perilipin, and type II keratin appeared in those samples. Starters with Pediococcus pentosaceus 31 from the Russian National Collection of Industrial Microorganisms (VKPM-8901) caused myoglobin and troponin I aggregation, while the formation of soy proteins aggregates (glycinin G1 and glyci- nin A3B4) was detected in meat products as a result of the autolysis process and the use of cholesterol-lowering star- ters. All in all, proteases which cause protein aggregation may be less effective for raw meat tenderization, whereas the proteins identified may be used as quality biomarkers.
Highlights
Protein aggregation in this paper is defined as the interaction of denatured protein molecules resulting in the formation of weak or strong molecular linkages
The proteomic analysis of raw meat revealed that animal proteases – pepsin and trypsin – caused the aggregation of isoform 2 of protein 1 containing 4.5 LIM domains
Proteases which cause protein aggregation may be less effective for raw meat tenderization, whereas the proteins identified may be used as quality biomarkers
Summary
Protein aggregation in this paper is defined as the interaction of denatured protein molecules resulting in the formation of weak or strong (for example, disulfide) molecular linkages. The results of the research conducted by Moszkowska et al [11] have shown the formation of protein aggregates in the muscle tissue packaged in an oxygen-containing atmosphere. These aggregates, which consist of myosin heavy chains, are the result of cross-linking proteins and are able to affect the meat tenderness adversely. Larger aggregates were observed in biceps femoris muscles in comparison to longissimus lumborum muscles and in meat packaged in the modified gas atmosphere (MGA) rather than in vacuum It may be explained by the metabolism of muscles analyzed due to differences in postmortem glycolysis extent, the characteristics of muscle fibers and their glycolytic and oxidative properties. 50 g raw meat and kept at 30°C for 40 min for trypsin and pepsin, and for 30 min for papain and bromeline
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