Identification of protein degradation during post-mortem storage of pig meat.
Eighteen proteins and peptides that were found to change post-mortem in Longissimus dorsi from pig muscle were identified by the use of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The 18 peptides originate from 9 different proteins including the 3 structural proteins (actin, myosin heavy chain, and troponin T) and the 6 metabolic proteins glycogen phosphorylase, creatine kinase, phosphopyruvate hydratase, myokinase, pyruvate kinase, and dihydrolipoamide succinyltransferase. The molecular weight and estimated sequence length of the identified spots show that these fragments result from proteolytic activity in meat. Identification of the parent proteins and the enhanced post-mortem appearance of the degradation products make these specific peptides good candidates for meat quality markers, and further studies of these specific fragments will lead to a better understanding of the proteolytic activities involved in the post-mortem conversion of muscle to meat.
Lametsch
René
R
Department of Animal Product Quality, Danish Institute of Agricultural Sciences, Tjele, Denmark.
Roepstorff
Peter
P
Bendixen
Emøke
E
D000818:Animals; D003402:Creatine Kinase / Q000737:chemistry / Q000378:metabolism; D015180:Electrophoresis, Gel, Two-Dimensional; D024981:Glycogen Phosphorylase / Q000737:chemistry / Q000378:metabolism; D008460:Meat; D008970:Molecular Weight; D009124:Muscle Proteins / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis / Q000737:chemistry / Q000378:metabolism; D010449:Peptide Mapping; D011180:Postmortem Changes; D011786:Quality Control; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013552:Swine
D009124:Muscle Proteins; D010446:Peptide Fragments; D024981:Glycogen Phosphorylase; D003402:Creatine Kinase