Rapid Post-Mortem Glycolysis and Delay Chilling of Turkey Carcasses Cause Alterations to Protein Extractability and Degradation of Breast Muscle Proteins
| Autor: | Mary D. Pato, Phyllis J. Shand, Bruce Rathgeber, Jane A. Boles |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Gel electrophoresis
Turkeys biology medicine.diagnostic_test Hydrolysis Blotting Western Muscle Proteins food and beverages General Chemistry Blot Glycogen phosphorylase Biochemistry Western blot Myosin biology.protein medicine Animals Electrophoresis Polyacrylamide Gel Glycolysis Creatine kinase Muscle Skeletal General Agricultural and Biological Sciences Myofibril |
| Zdroj: | Journal of Agricultural and Food Chemistry. 47:2529-2536 |
| ISSN: | 1520-5118 0021-8561 |
| DOI: | 10.1021/jf981272c |
| Popis: | SDS-PAGE banding patterns of myofibrillar protein samples from turkey breast muscle with pHor =5.8 at 15 min post-mortem (rapid glycolyzing) contained 133, 142, and 165 kDa bands that were absent in samples from carcasses with pH6.0 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. |
| Databáze: | OpenAIRE |
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