Abstract
The aim of this research was to correlate the postmortem changes of sarcoplasmic proteins with instrumental color and various biochemical parameters relating to color attributes. Two-dimensional electrophoresis was used to investigate sarcoplasmic protein changes in cardiac muscle during refrigerated storage. Eleven differentially abundant protein spots were identified between storage time at day 1 and day 5 (PÂ <Â 0.05). The functional category of proteins consisted of metabolic enzymes, binding proteins, chaperone proteins, and antioxidant proteins. These proteins demonstrated positive correlation with a*-value (creatine kinase M-type and malate dehydrogenase), metmyoglobin-reducing activity (aconitate hydratase, creatine kinase, and thioredoxin-dependent peroxide reductase), tissue oxygen consumption rate (creatine kinase and malate dehydrogenase), and mitochondrial respiration control ratio (thioredoxin-dependent peroxide reductase and mitochondrial superoxide dismutase). The protein patterns were likely to have impact on postmortem metabolism, thereby protecting muscle against discoloration.
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Acknowledgments
We gratefully acknowledge the financial support by Nature Science Foundation of Hebei province China (Project No: C2015208052), Science and technology research project of Hebei Education Department (Project No: QN2015120) and the Ministry of Agriculture of China (China Agriculture Research System-39, CARS-39).
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Gao, X., Wu, W., Ma, C. et al. Postmortem changes in sarcoplasmic proteins associated with color stability in lamb muscle analyzed by proteomics. Eur Food Res Technol 242, 527–535 (2016). https://doi.org/10.1007/s00217-015-2563-2
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DOI: https://doi.org/10.1007/s00217-015-2563-2