Early post-mortem degradation of intramuscular collagen

Mills, Edward W.; Smith, S. H.; Judge, M. D.

doi:10.1016/0309-1740(89)90034-x

Cited by 18 publications

(3 citation statements)

References 15 publications

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“…Again, as for total collagen, this could be due to a location effect but proteolysis upon aging could be the responsible factor. A recent study reinforces that assumption (Mills et al, 1989) by showing an increase in soluble collagen in the first 12 hr after slaughter. In this current study, ES did not affect soluble collagen significantly but fast chilling tended to reduce the amount of soluble collagen (P = 0.0887).…”

Section: Collagensupporting

confidence: 73%

Vitamin A, Electrical Stimulation, and Chilling Rate Effects on Lysosomal Enzyme Activity in Aging Bovine Muscle

Pommier

1992

Journal of Food Science

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Means of enhancing the rate of aging of bovine meat were investigated to provide some understanding of the tenderization process. Vitamin A was administered to finishing steers, carcasses were electrically stimulated, and longissimus dorsi muscle samples chilled at 2 different rates. Liver cathepsin D, beta-glucuronidase and hexosaminidase were increased (PcO.05) with vitamin A supplementation but muscle enzymes were not affected. Chilling rate, electrical stimulation and time significantly (PcO.05) affected cathepsin D distribution patterns, meat color, Warner-Bratzler, myofibrillar fragmentation index and collagen data. Troponin-T degradation was enhanced by aging. Thus, vitamin A can modify liver catheptic enzyme activity but does not affect muscle enzymes at these levels.

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Section: Collagensupporting

confidence: 73%

Vitamin A, Electrical Stimulation, and Chilling Rate Effects on Lysosomal Enzyme Activity in Aging Bovine Muscle

Pommier

1992

Journal of Food Science

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“…Studies from Bailey's laboratory, however, have indicated that it is not only the quantity of collagen but also the amount of cross-linking, the nature, and the solubility properties of the collagen present in a muscle that play a role in determining meat toughness and texture (Bailey, 1984;Light et al, 1985). Recent studies by Mills et al (1989) have shown that thermal stability of collagen declined while muscle collagen solubility increased during the first 24 h after slaughter. In addition, the physical characteristics of extracellular matrix connective tissue proteins changed.…”

Section: Resultsmentioning

confidence: 99%

Effect of dietary restriction during gestation on amino acid composition and myofibrillar and collagen contents of skeletal muscle in gilts mated at puberty

Zarkadas¹,

Larmond²,

Elliot³

et al. 1992

J. Agric. Food Chem.

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“…Collagen degradation has been examined in relation to glue (Saban et al, 1992), meat tenderization (e.g. Mills et al, 1989), and the stability of collagen haemostatics and sutures (Rudakova & Zaikov, 1987).…”

Section: Previous Studies Of Collagen Degradationmentioning

confidence: 99%