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R. Lawrie, J. Sharp, J. Bendall, B. Coleby (1961)
Treatment of meats with ionising radiations. VIII.—pH, water‐binding capacity and proteolysis of irradiated raw beef and pork during storage, and the ATP‐ase activity of irradiated rabbit muscleJournal of the Science of Food and Agriculture, 12
Deatherage Deatherage, Hamm Hamm (1960)
Influence of freezing and thawing on hydration and charges of the muscle proteinsFood Research, 25
Folin Folin, Ciocalteu Ciocalteu (1927)
On tyrosine and tryptophane in proteinsJ. Biol. Chem, 73
Bradley Bradley, Bailey Bailey (1940)
Estimation of decomposition of fish muscleFood Res, 5
Hunt Hunt, Matheson Matheson (1958)
The effect of dehydration on actomyosin in fish and beef muscleFood Technol, 12
A. Khan (1962)
Extraction and Fractionation of Proteins in Fresh Chicken MuscleaJournal of Food Science, 27
B. Lowe (1948)
Factors Affecting the Palatability of Poultry with Emphasis on Histological Post-mortem ChangesAdvances in food research, 1
Slinwinski Slinwinski, Doty Doty, Landmann Landmann (1959)
Over‐all assay and partial purification procedures for proteolytic enzymes in beef muscleAgr. Food Chm, 7
F. Deatherage, R. Hamm (1960)
INFLUENCE OF FREEZING AND THAWING ON HYDRATION AND CHARGES OF THE MUSCLE PROTEINSaJournal of Food Science, 25
Bandack‐Yuri Bandack‐Yuri, Rose Rose (1961)
Proteases of chicken breast muscleFood Technol, 15
Russell Allen (1940)
The estimation of phosphorus.The Biochemical journal, 34 6
Greville Greville, Tapley Tapley (1960)
Effects of phenyl‐mercuric acetate on the enzymatic activity of l‐myosinBiochem. J, 76
R. Love (1962)
Protein denaturation in frozen fish. VI.—Cold‐storage studies on cod using the cell fragility methodJournal of the Science of Food and Agriculture, 13
Ball Ball (1938)
Enzyme action in food products at low temperaturesIce and Cold Storage, 41
H. Bkadley, B. Bailey (1940)
ESTIMATION OF DECOMPOSITION OF FISH MUSCLEJournal of Food Science, 5
Partmann Partmann (1959)
Versuch einer structurellen und funktionellene analysis von gefrierbrandschaden bie geflugelFleischwirtschaft, 11
O. Folin, V. Ciocalteu (1927)
ON TYROSINE AND TRYPTOPHANE DETERMINATIONS IN PROTEINSJournal of Biological Chemistry, 73
Stewart Stewart, Lowe Lowe (1948)
Producing and maintaining quality in frozen eviscerated poultryFrosen Food Ind, 4
Bate‐Smith Bate‐Smith (1948)
The physiology and chemistry of rigor mortis with special reference to aging of beefAdvances in Food Research, 1
Stewart Stewart, Hanson Hanson, Lowe Lowe (1945)
Effect of aging, freezing rate, and storage period on palatability of broilersFood Research, 10
Gutschmidt Gutschmidt (1959)
Untersuchungen über die gefrierlagerung von hähnchenKältetechnik, 11
Pool Pool, Fremery Fremery, Campbell Campbell, Klose Klose (1959)
Poultry tenderness. II. Influence of processing on tenderness of chickensFood Technol, 13
J. Connell (1960)
Changes in the actin of cod flesh during storage at −14°Journal of the Science of Food and Agriculture, 11
H. Harshaw, Walter Hale, L. Alexander, R. Slocum (1941)
Quality of Frozen Poultry as Affected by Storage and Other ConditionsResearch Papers in Economics
Stewart Stewart, Hanson Hanson, Lowe Lowe (1943)
Palatability studies on poultry: a comparison of three methods for handling poultry prior to eviscerationFood Research, 8
J. Blum (1960)
Interaction between myosin and its substrates.Archives of biochemistry and biophysics, 87
Hyman Rosen (1957)
A modified ninhydrin colorimetric analysis for amino acids.Archives of biochemistry and biophysics, 67 1
G. Stewart, H. Hanson, B. Lowe, Joseph Austin (1945)
EFFECTS OF AGING, FREEZING RATE, AND STORAGE PERIOD ON PALATABILITY OF BROILERSJournal of Food Science, 10
G. Stewart, H. Hanson, B. Lowe (1943)
Palatability studies on poultry: a comparison of three methods for handling poultry prior to evisceration.Journal of Food Science, 8
S. Perry (1961)
The Biochemistry of MuscleAnnual Review of Biochemistry, 30
B. Coleby, M. Ingram, H. Shepherd, M. Thornley, G. Wilson (1961)
Treatment of meats with ionising radiations. VII.—effect of low temperatures during irradiation†Journal of the Science of Food and Agriculture, 12
Khan Khan (1962a)
Some observations on biochemical changes in chicken muscle proteins during frozen storageProc. Can. Fed. Biol. Soc, 5
R. Śliwiński, D. Doty, W. Landmann (1959)
Enzymes in Beef Muscle, Over-All Assay and Partial Purification Procedures for Proteolytic Enzymes in Beef MuscleJournal of Agricultural and Food Chemistry, 7
SUMMARY Quantitative examination of chicken muscle proteins showed that protein extractability in both breast and leg muscle decreased during frozen storage because of loss of solubility of actomyosin fraction. This decrease accompanied a decrease in the sulfhydryl‐group content of muscles and loss in myosin‐adenosinetriphosphatase activity. The stroma‐protein fraction remained unaffected, and the sarcoplasmic‐protein fraction decreased only after long storage. In the non‐protein‐nitrogen fraction, the amount of free amino acids and other protein‐breakdown products increased as a result of proteolysis. The rate of these changes depended directly on storage temperature and time. It is suggested that chicken muscles in frozen storage undergo proteolysis and that the myofibrillar‐protein fraction is denatured.
Journal of Food Science – Wiley
Published: Jul 1, 1963
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