Rapid post-mortem glycolysis and delay chilling of turkey carcasses cause alterations to protein extractability and degradation of breast muscle proteins.
SDS-PAGE banding patterns of myofibrillar protein samples from turkey breast muscle with pH < or =5.8 at 15 min post-mortem (rapid glycolyzing) contained 133, 142, and 165 kDa bands that were absent in samples from carcasses with pH >6.0 at 15 min post-mortem (normal glycolyzing). These extra protein bands contained fragments of myosin as identified by Western blot analysis. Myosin fragments were also observed in protein samples from breast muscle not allowed to cool until 110 min post-mortem (delay chilled). In addition to myosin degradation, neublin degradation was more extensive in samples from rapid glycolyzing carcasses than for normal controls. Creatine kinase and glycogen phosphorylase were present in myofibrillar protein extracts of rapid glycolyzing carcasses in higher quantities than in normal controls. Results of this study provide insight into the molecular basis for previously reported reductions in meat quality of rapid glycolyzing and delay chilled turkey meat.
Rathgeber
B M
BM
Department of Applied Microbiology and Food Science and Department of Biochemistry, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5A8, Canada.
Pato
M D
MD
Boles
J A
JA
Shand
P J
PJ
D000818:Animals; D015153:Blotting, Western; D004591:Electrophoresis, Polyacrylamide Gel; D006019:Glycolysis; D006868:Hydrolysis; D009124:Muscle Proteins / Q000737:chemistry* / Q000302:isolation & purification; D018482:Muscle, Skeletal / Q000737:chemistry*; D014422:Turkeys
D009124:Muscle Proteins