Journal ArticleDOI
Photomicrographic Studies of Dynamic Changes in Muscle Fiber Fragments. 1. Effect of Various Heat Treatments on Length, Width and Birefringence
R. L. Hostetler,W. A. Landmann +1 more
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TLDR
In this article, the possible relationship of changes in width, length and in birefringence brought about by heating to loss of moisture, water-holding properties, loss of acidic groups, and changes in tenderness are discussed.Abstract:
SUMMARY– Photomicrographs were made of muscle fiber fragments as the stage of the microscope was heated from room temperature to 80°C, or as fibers were held at 37, 45, 53, 61, 69, or 77°C on the heated stage for an hour. The possible relationship of changes in width, length and in birefringence brought about by heating to loss of moisture, water-holding properties, loss of acidic groups, and changes in tenderness are discussed. Changes in width appeared to be related to changes in water-holding capacity. Changes in length and loss of birefringence were related to loss of acidic groups, to coagulation of proteins, to volume change in cooked meat, and to changes in tenderness.read more
Citations
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Journal ArticleDOI
Effects of heat on meat proteins – Implications on structure and quality of meat products
TL;DR: The structural changes on cooking in whole meat and comminuted meat products, and the alterations in water-holding and texture of the meat product that it leads to, are discussed.
Journal ArticleDOI
A theoretical approach of the relationships between collagen content, collagen cross-links and meat tenderness.
TL;DR: The decisive role of rubber-like properties of connective tissues in meat tenderness variations is demonstrated, i.e. pressure and elastic modulus follows most of the variations of meat toughness.
Journal ArticleDOI
The cooking of single myofibres, small myofibre bundles and muscle strips from beef M. psoas and M. sternomandibularis muscles at varying heating rates and temperatures.
J.R. Bendall,D.J. Restall +1 more
TL;DR: When single myofibres are heated in an aqueous medium up to temperatures of 90°C at pH 5·5, they do n ot shorten but instead decrease in diameter, which leads to a volume decrease and a loss of about 68% of the cell water.
Journal ArticleDOI
Systematic review of emerging and innovative technologies for meat tenderisation.
Robyn D. Warner,Ciara K. McDonnell,A.E.D. Bekhit,James R. Claus,Rozita Vaskoska,Anita L. Sikes,Frank R. Dunshea,Minh Ha +7 more
TL;DR: In the future, a combination of new and innovative technologies will be ideally suited to deliver a range of desired textures for meat products.
Journal ArticleDOI
Effects of animal age, marbling score, calpastatin activity, subprimal cut, calcium injection, and degree of doneness on the palatability of steaks from limousin steers.
TL;DR: Shear force was lowest between "medium rare" and "medium" and increased toward both ends of the degree of doneness scale for round and sirloin steaks; however, shear force increased linearly with degree ofDoneness in strip loin steaks (P < .05).
References
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Journal ArticleDOI
CHANGES IN HYDRATION, SOLUBILITY AND CHARGES OF MUSCLE PROTEINS DURING HEATING OF MEATa
Reiner Hamm,F. E. Deatherage +1 more
Journal ArticleDOI
The Effect of Heating Time and Temperature on the Shear of Beef Semitendinosus Muscle a
S. M. Machlik,H. N. Draudt +1 more
TL;DR: Relatively large differences, attributed to undefined biological differences, were noted in the shear versus heating time patterns for semitendinosus muscle cylinders from different animals.
Journal ArticleDOI
The dissociation of myosin by heat coagulation.
TL;DR: When myosin solutions were coagulated at 53°, pH 6.2, 8–18% of the protein remained in solution, and the adenylic deaminase activity of P was 3–4 times greater than that of myOSin while that of D was low.
Journal ArticleDOI
The Histology of Pre-Rigor and Post-Rigor Ox Muscle Before and After Cooking and Its Relation to Tenderness
TL;DR: It was concluded that, provided the effects of gross connective tissue are small, tenderness in beef muscle is produced by disruption of the actin filaments and by a breaking down of the linkages between theActin and myosin Filaments in the sarcomeres.
Journal ArticleDOI
Heat Induced Changes of Moisture in Turkey Muscles
TL;DR: In this paper, the effects of end point temperature in unheated (10°C) muscle and muscle heated (dry heat, 176°C), to 25, 35, 45, 55 and 65°C on moisture measured by selected methods, Warner-Bratzler shear values, and pH values of breasts and thigh-legs from tom turkeys were investigated.
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