Abstract
The objective of this study was to investigate the proteomic characteristics for the sarcoplasmic and myofibrillar proteomes of M. longissimus lumborum (LL) and M. psoasmajor (PM) from Small-tailed Han Sheep. During post-mortem storage periods (1, 3, and 5 days), proteome analysis was applied to elucidate sarcoplasmic and myofibrillar protein changes in skeletal muscles with different color stability. Proteomic results revealed that the identified differentially abundant proteins were glycolytic enzymes, energy metabolism enzymes, chaperone proteins, and structural proteins. Through Pearson’s correlation analysis, a few of those identified proteins (Pyruvate kinase, Adenylate kinase isoenzyme 1, Creatine kinase M-type, and Carbonic anhydrase 3) were closely correlated to representative meat color parameters. Besides, bioinformatics analysis of differentially abundant proteins revealed that the proteins mainly participated in glycolysis and energy metabolism pathways. Some of these proteins may have the potential probability to be predictors of meat discoloration during post-mortem storage. Within the insight of proteomics, these results accumulated some basic theoretical understanding of the molecular mechanisms of meat discoloration.
Highlights
Among various sensory characteristics, the color of fresh meat is a critical quality factor, influencing the purchase decision of the consumers [1]
In the present research, the post-mortem proteome profiles associated with the typical color-stable (M. longissimus lumborum) and color-labile (M. psoasmajor) muscles of Small-tailed Han Sheep were studied and compared
The results of differential proteome indicated that the identified proteins were glycolytic enzymes, energy metabolism en
Summary
The color of fresh meat is a critical quality factor, influencing the purchase decision of the consumers [1]. Because of the distinct metabolic function and biochemical profile, M. longissimus lumborum (LL) and M. psoas major (PM) were considered to be typical color-stable and color-labile muscles, respectively, by previous researchers [9,10]. Both of the skeletal muscles whose color stabilities (color-stable and color-labile) were opposing can be used as typical experimental subjects to elaborate the underlying biochemical mechanisms of post-mortem color stability [11]. The objective of this study was to investigate the proteomic characteristics for the sarcoplasmic and myofibrillar proteome of M. longissimus lumborum (LL) and M. psoasmajor (PM) from Small-tailed Han Sheep during post-mortem storage
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