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

Samples were removed from bovine longissimus (L), semitendinosus (ST) and psoas major (PM) muscles at 1, 2, 3, 6, 7, 10 or 13 days postmortem stored at 2°C or 25°C. Myofibril fragmentation index (MFI) and Warner-Bratzler (W-B) shear-force values were determined on steaks from each muscle. Myofibril fragmentation index (MFI) was determined quantitatively by measuring the absorbance of a myofibril suspension. It was observed that MFI increased during postmortem storage for L and ST, but increased only slightly for PM. These results paralleled those changes in myofibrils observed with phase and polarized light microscopy. Both MFI and W-B shear-force values changed greatly from 1 to 3 days postmortem with a lesser change occurring after 3 days in L and ST muscles. In PM muscle, however, only a slight change in MFI and W-B shear-force occurred during postmortem storage. Elevated storage temperature (25°C) caused an accelerated change in both MFI and W-B shear-force in L and ST muscles; however, storage temperature had little effect on PM muscle. L and ST muscles responded similarly to postmortem storage, but PM muscle was characteristically different from the L and ST muscles. These findings demonstrate the differences and similarities of muscles to postmortem storage and further elucidate the role of myofibrillar proteins in meat tenderness.

[1]  T. Vestergaard,et al.  MYOFIBRIL FRAGMENTATION IN BOVINE LONGISSIMUS DORSI AS AN INDEX OF TENDERNESS , 1973 .

[2]  R. B. Young,et al.  EFFECT OF POSTMORTEM CONDITIONS ON CERTAIN CHEMICAL, MORPHOLOGICAL AND ORGANOLEPTIC PROPERTIES OF BOVINE MUSCLE , 1973 .

[3]  R. Currie,et al.  EFFECT OF POSTMORTEM AGING ON CHICKEN MUSCLE LIPIDS , 1973 .

[4]  D. E. Goll,et al.  Tryptic Digestion of Muscle Components Simulates Many of the Changes Caused by Postmortem Storage , 1971 .

[5]  G. Smith,et al.  EFFECTS OF PHYSICAL AND MECHANICAL TREATMENTS ON THE TENDERNESS OF THE BEEF LONGISSIMUS , 1971 .

[6]  D. W. Henderson,et al.  A comparison of shortening and Z line degradation in post-mortem bovine, porcine, and rabbit muscle. , 1970, The American journal of anatomy.

[7]  R. N. Sayre.  Chicken Myofibril Fragmentation in Relation to Factors Influencing Tenderness , 1970 .

[8]  E. Briskey,et al.  Treatment and Post‐Mortem Aging Effects on the Z‐line of Myofibrils from Chicken Pectoral Muscle , 1969 .

[9]  R. E. Rust,et al.  Effect of postmortem aging time and temperature on beef muscle attributes. , 1969, Journal of animal science.

[10]  K. V. Gilbert,et al.  Studies in Meat Tenderness. 7. Changes in the Fine Structure of Meat During Aging , 1969 .

[11]  D. E. Goll,et al.  MORPHOLOGY OF RIGOR-SHORTENED BOVINE MUSCLE AND THE EFFECT OF TRYPSIN ON PRE- AND POSTRIGOR MYOFIBRILS , 1967, The Journal of cell biology.

[12]  Koui Takahashi,et al.  Formation of Myofibrillar Fragments and Reversible Contraction of Sarcomeres in Chicken Pectoral Muscle , 1967 .

[13]  D. E. Goll,et al.  Molecular Properties of Post‐Mortem Muscle. 4. Effect of Temperature on Adenosine Triphosphate Degradation, Isometric Tension Parameters, and Shear Resistance of Bovine Muscle , 1967 .

[14]  K. V. Gilbert,et al.  Structural changes in meat during ageing , 1967 .

[15]  R. H. Locker.  DEGREE OF MUSCULAR CONTRACTION AS A FACTOR IN TENDERNESS OF BEEF , 1960 .

[16]  A. Gornall,et al.  Determination of serum proteins by means of the biuret reaction. , 1949, The Journal of biological chemistry.