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D. Goll, R. Robson, J. Temple, M. Stromer (1971)
An effect of trypsin on the actin-myosin interaction.Biochimica et biophysica acta, 226 2
Koui Takahashi, T. Fukazawa, T. Yasui (1967)
Formation of Myofibrillar Fragments and Reversible Contraction of Sarcomeres in Chicken Pectoral MuscleJournal of Food Science, 32
M. Stromer, D. Goll, L. Roth (1967)
MORPHOLOGY OF RIGOR-SHORTENED BOVINE MUSCLE AND THE EFFECT OF TRYPSIN ON PRE- AND POSTRIGOR MYOFIBRILSThe Journal of Cell Biology, 34
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Further Studies on Bovine Muscle Tenderness as Influenced by Carcass Position, Sarcomere Length, and Fiber DiameterJournal of Food Science, 30
D. Henderson, D. Goll, M. Stromer (1970)
A comparison of shortening and Z line degradation in post-mortem bovine, porcine, and rabbit muscle.The American journal of anatomy, 128 1
Toshiyuki Fukazawa, Tsutomu Yasui (1967)
The change in zigzag configuration of the Z-line of myofibrils.Biochimica et biophysica acta, 140 3
D. Goll, M. Stromer, R. Robson, J. Temple, B. Eason, W. Busch (1971)
Tryptic Digestion of Muscle Components Simulates Many of the Changes Caused by Postmortem StorageJournal of Animal Science, 33
C. Davey, K. Gilbert (1967)
Structural changes in meat during ageingInternational Journal of Food Science and Technology, 2
R. Sayre (1970)
Chicken Myofibril Fragmentation in Relation to Factors Influencing TendernessJournal of Food Science, 35
Goll Goll, Robson Robson (1967)
Molecular properties of postmortem muscle. 1. Myo‐fibrillar nucleosidetriphosphatase activity of bovine muscleJ. Food Sci., 32
W. Busch, M. Stromer, D. Goll, Atsushi Suzuki (1972)
Ca2+-SPECIFIC REMOVAL OF Z LINES FROM RABBIT SKELETAL MUSCLEThe Journal of Cell Biology, 52
Rey Rey, Kraft Kraft, Walker Walker, Parrish Parrish (1970)
Microbial changes in meat during aging at elevated temperature and later refrigerated storageFood Tech-nol., 24
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Effect of postmortem aging time and temperature on beef muscle attributes.Journal of animal science, 29 3
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Histological Studies of Post-Mortem Changes in Sarcomere Length as Related to Bovine Muscle TendernessJournal of Food Science, 31
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Shrinkage and organoleptic characteristics of beef aged in controlled environmentsFood Technol., 12
Stromer Stromer, Goll Goll (1967a)
Molecular properties of postmortem muscle. 11. Phase microscopy of myofibrils from bovine muscleJ. Food Sci., 32
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T. Moran, J. Pace (1967)
Bread as a source of proteinInternational Journal of Food Science and Technology, 2
C. Davey, M. Dickson (1970)
Studies in Meat Tenderness 8. Ultra-structural Changes in Meat During AgingJournal of Food Science, 35
N. Arakawa, D. Goll, J. Temple (1970)
MOLECULAR PROPERTIES OF POSTMORTEM MUSCLE. 8. Effect of Postmortem Storage on α‐Actinin and the Tropomyosin‐Troponin ComplexJournal of Food Science, 35
A. Gornall, C. Bardawill, M. David (1949)
Determination of serum proteins by means of the biuret reaction.The Journal of biological chemistry, 177 2
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Isolation of structural elements of food products by preparative ultracentrifugation: ice cream and ice‐cream mix *International Journal of Food Science and Technology, 2
Sleeth Sleeth, Henrickson Henrickson, Brady Brady (1957)
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F. Parrish, D. Goll, W. Newcomb, B. Lumen, H. Chaudhry, E. Kline (1969)
Molecular Properties of Post‐Mortem Muscle. 7. Changes in Nonprotein Nitrogen and Free Amino Acids of Bovine MuscleJournal of Food Science, 34
Herring Herring, Cassens Cassens, Suess Suess, Brun‐gardt Brun‐gardt, Briskey Briskey (1967)
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Locker Locker (1960)
Degree of muscular contraction as a factor in tenderness of beefFood Res., 25
W. Busch, F. Parrish, D. Goll (1967)
Molecular Properties of Post‐Mortem Muscle. 4. Effect of Temperature on Adenosine Triphosphate Degradation, Isometric Tension Parameters, and Shear Resistance of Bovine MuscleJournal of Food Science, 32
T. Fukazawa, E. Briskey, F. Takahashi, T. Yasui (1969)
Treatment and Post‐Mortem Aging Effects on the Z‐line of Myofibrils from Chicken Pectoral MuscleJournal of Food Science, 34
Robson Robson, Goll Goll, Temple Temple (1968)
Determination of proteins in “Tris” buffer by the biuret reactionAnal. Bio-chem., 24
Marsh Marsh, Woodhams Woodhams, Leet Leet (1968)
Studies in meat tenderness. 5. The effects on tenderness of carcass cooling and freezing before the completion of rigor mortisJ. Food Sci., 34
R. Howard, M. Judge (1968)
Comparison of Sarcomere Length to Other Predictors of Beef TendernessJournal of Food Science, 33
C. Davey, K. Gilbert (1969)
Studies in Meat Tenderness. 7. Changes in the Fine Structure of Meat During AgingJournal of Food Science, 34
H. Herring, R. Cassens, E. Briskey (1965)
Sarcomere length of free and restrained bovine muscles at low temperature as related to tendernessJournal of the Science of Food and Agriculture, 16
R. Locker (1960)
DEGREE OF MUSCULAR CONTRACTION AS A FACTOR IN TENDERNESS OF BEEFJournal of Food Science, 25
D. Goll, D. Henderson, E. Kline (1964)
Post-Mortem Changes in Physical and Chemical Properties of Bovine MuscleaJournal of Food Science, 29
S. McCrae, Cherie Seccombe, B. Marsh, W. Carse (1971)
STUDIES IN MEAT TENDERNESS. 9. The Tenderness of Various Lamb Muscles in Relation to Their Skeletal Restraint and Delay Before FreezingJournal of Food Science, 36
P. Heaps, T. Webb, P. Eggitt, J. Coppock (1967)
Studies on mechanical factors affecting dough developmentInternational Journal of Food Science and Technology, 2
M. Stromer, D. Goll (1967)
Molecular Properties of Post-Mortem Muscle. 3. Electron Microscopy of MyofibrilsJournal of Food Science, 32
J. Schmidt, F. Parrish (1971)
MOLECULAR PROPERTIES OF POSTMORTEM MUSCLE. 10. Effect of Internal Temperature and Carcass Maturity on Structure of Bovine LongissimusJournal of Food Science, 36
Paired sides from U.S. Choice grade beef were aged immediately after slaughter at 2 and 16°C. Samples were removed from longissimus and semitendinosus at slaughter and at 1, 3 and 7 days postmortem for ATPase assay, phase microscopy, shear and organoleptic evaluation. Rib steaks from sides aged at 16°C for 1‐day postmortem were as tender as steaks from sides aged at 2°C for 7 days postmortem. Flavor development of rib steaks also was more rapid at 16°C than at 2°C. Tenderness of semitendinosus steaks was improved by aging sides at 16°C; the difference in improvement of tenderness of semitendinosus, however, was not as great between 2°nd 16° as it was for rib steaks. Ca++, Mg++ and EGTA‐modified ATPase activity of myofibrils from both muscles increased with postmortem time, with myofibrils from muscles held at 16°C having slightly higher ATPase activity than myofibrils from muscles held at 2° Increased EGTA‐modified ATPase activity was indicative of loss of calcium sensitivity of the myofibril. Sarcomeres of myofibrils from longissimus were longer at 1‐day postmortem than those from at‐death longissimus and they remained essentially unchanged during the remainder of postmortem aging; however, tenderness improved at 16°C for 1 day and at 2°C for 3 days. Also greater fragmentation of myofibrils from longissimus postmortem aged at 16°C for 1 day and at 2°C for 3 days was observed, suggesting that the rate of myofibril fragmentation is an important factor in tenderization.
Journal of Food Science – Wiley
Published: May 1, 1973
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