MYOFIBRIL FRAGMENTATION AND SHEAR RESISTANCE OF THREE BOVINE MUSCLES DURING POSTMORTEM STORAGE

Journal of Food Science

Volumn 41, Issue 5, 1976, Pages 1036-1041

  OLSON, DENNIS G ^a   JR , F C PARRISH ^a   STROMER, M H ^a  

^a IOWA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84985057777     PISSN: 00221147     EISSN: 17503841     Source Type: Journal    
DOI: 10.1111/j.1365-2621.1976.tb14384.x     Document Type: Article

References (17)

1. Molecular properties of postmortem muscle. 4. Effect of temperature on adenosine triphosphate degradation, isometric tension parameters, and shear resistance of bovine muscle
2. Structural changes in meat during aging
3. Studies in meat tenderness. 7. Changes in the fine structure of meat during aging
4. Treat ment and post‐mortem aging effects on the Zline from chicken pectoral muscle
5. Tryptic digestion of muscle components simulates many of the changes caused by postmortem storage
6. Determination of serum proteins by means of the biuret reagent
7. Effect of postmortem aging on chicken myofibrils
8. A comparison of shortening and Zline degradation in postmortem bovine, porcine, and rabbit muscle
9. Degree of muscular contraction as a factor in tenderness of beef
10. Myofibril fragmentation in bovine longissimus dorsi as an index of tenderness
11. Effect of postmortem aging time and temperature on beef muscle attributes
12. Effect of postmortem conditions on certain chemical, morphological and organoleptic properties of bovine muscle
13. Chicken myofibril fragmentation in relation to factors influencing tenderness
14. Effects of physical and mechanical treatments on the tenderness of the beef longissimus
15. Morphology of rigorshortened bovine muscle and the effect of trypsin on pre‐ and post‐rigor myofibrils
16. Formation of myofibrillar fragments and reversible contraction of sarcomere in chicken pectoral muscle