Monitoring post mortem changes in porcine muscle through 2-D DIGE proteome analysis of Longissimus muscle exudate

Abstract

BackgroundMeat quality is a complex trait influenced by a range of factors with post mortem biochemical processes highly influential in defining ultimate quality. High resolution two-dimensional DIfference Gel Electrophoresis (2-D DIGE) and Western blot were applied to study the influence of post mortem meat ageing on the proteome of pork muscle. Exudate collected from the muscle following centrifugation was analysed at three timepoints representing a seven day meat ageing period.ResultsThe intensity of 136 spots varied significantly (p < 0.05) across this post mortem period and 40 spots were identified using mass spectrometry. The main functional categories represented were metabolic proteins, stress-related proteins, transport and structural proteins. Metabolic and structural proteins were generally observed to increase in abundance post mortem and many likely represent the accumulation of the degradation products of proteolytic enzyme activity. In contrast, stress-related proteins broadly decreased in abundance across the ageing period. Stress response proteins have protective roles in maintaining cellular integrity and a decline in their abundance over time may correlate with a reduction in cellular integrity and the onset of meat ageing. Since cellular conditions alter with muscle ageing, changes in solubility may also contribute to observed abundance profiles.ConclusionsMuscle exudate provided valuable information about the pathways and processes underlying the post mortem ageing period, highlighting the importance of post mortem modification of proteins and their interaction for the development of meat quality traits.

Protein profile and physicochemical characteristics of meat of lambs fed diets supplemented with rapeseed oil, fish oil, carnosic acid, and different chemical forms of selenium

“…Di Luca et al (2013b) stated that muscle exudate could be a good source of these proteins because it provides valuable information about the pathways and processes underlying the post mortem ageing period as well as highlighting its post mortem modifications. Some studies have also shown that sarcoplasmic protein profile in drip loss is also determined by the feeding of animals (Shibata et al, 2009;Costa-Lima et al, 2015).…”

The relationship between protein changes in porcine longissimus muscle at different courses of meat tenderisation

“…Rapid development of proteomics involves the application of various electrophoretic techniques [12,14,52,55], which allow the identification of many proteins with respect to their properties. It leads to better understanding of the causes and consequences of the phenomena influencing the quality of meat, especially its tenderness [15,20,22,31,32,35,40,47,51].…”

Effect of Pre-Slaughter Autophagic Status on Postmortem Proteolysis in Skeletal Muscle of Mice

“…Although water-soluble sarcoplasmic proteins are not structural proteins in skeletal muscle, their post mortem proteolysis has been shown to occur in parallel with tenderization of meat (Bowker et al, 2008). Moreover, the water-soluble fraction contains fragments of myofibrillar proteins, which become extractable by post mortem proteolysis (Di Luca et al, 2013). Therefore, post mortem changes in water-soluble proteins are considered useful indicators of meat tenderness.…”