Post‐Mortem Changes in Protein Extractability in Beef, Pork, and Chicken Muscle

McINTOSH, Elaine Nelson

doi:10.1111/j.1365-2621.1967.tb01295.x

Cited by 12 publications

(12 citation statements)

References 5 publications

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“…After a certain minimal level of actomyosin is reached, there is roughly a linear correlation between actomyosin content and emptying. The yield of actomyosin was similar to that found by other workers using this method (13), and recovery of protein from the various fractions was 100 5%. Since the actomyosin determinations were performed under an entirely different set of extracting conditions than the emptying, the two sets of data do not merely reflect two measures of the same phenomenon.…”

supporting

confidence: 87%

Mechanism of Emptying of Skeletal Muscle Cell Segments

Stanley

Hultin

1968

The Journal of Cell Biology

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supporting

confidence: 87%

Mechanism of Emptying of Skeletal Muscle Cell Segments

Stanley

Hultin

1968

The Journal of Cell Biology

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“…It has been shown that sarcoplasmic proteins d o not undergo large changes in compoosition during postmortem storage at 5 C or lower (Aberle and Merkel, 1966;Lawrie et al, 1963;Scopes, 1964). The extractability of the myofibrillar proteins has been shown t o increase up to 2 wk postmortem (Aberle and Merkel, 1966;McIntosh, 1967). Davey and Gilbert (1968a) reported an increase in the myofibrillar protein extract during aging of beef and rabbit muscle.…”

Section: Introductionmentioning

confidence: 99%

PROTEOLYTIC ACTIVITY OF Pseudomonas perolens AND EFFECTS ON PORCINE MUSCLE

Buckley

Gann

Price

et al. 1974

Journal of Food Science

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S Changes in the solubility of the primary muscle proteins attributable to the presence and growth of Pseudomonas perolens were increases in the extractability of myofibrillar and nonprotein nitrogen components at the expense of the sarcoplasmic and stroma proteins. Initiation of the production of high levels of proteolytic enzyme by Pseudomonas perolens in inoculated pork occurred concurrently with a rapid rise in pH and the peak of the bacterial growth curve. Incubation of porcine muscle at 3°C with or without bacterial cells resulted in minor ultrastructural changes. The purified proteolytic enzyme extract produced by Pseudomonas perolens appeared to cause the removal of the Z line and M line after as little as 4 days incubation. Fragmentation of the myofibrils and disintegration of actin filaments was evident after 8 days. Those samplcs containing bacterial cells exhibited varying degrees of ultrastructural damage after 8 days incubation. Localized disruption of myofibrils was observed and may have been due to localized growth or enzyme claboration of bacterial cells.

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“…An early survey showed no gross changes in total mucoprotein hexosamine (McIntosh, 1961), collagen, elastin, or total nitrogen. Failure to find changes in total amount of connective-tissue components supported the view that the visual changes observed might be a reflection of much more subtle changes, probably structural in nature.…”

Section: -Journalmentioning

confidence: 96%

“…At the end of the designated aging period, these muscles were also wrapped and frozen. Later, the frozen muscles were thawed, and the mucoprotein fraction was isolated essentially as described earlier (McIntosh, 1965) except that precipitation by aminoacridine hydrochloride was conducted at pH 7 in an attempt to minimize protein degradation. With this modification, the resultant products had higher viscosity and lower hexosamine content than those found previously (McIntosh, 1966).…”

Section: Meat Samplesmentioning

confidence: 99%

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Effect of Post‐Mortem Aging and Enzyme Tenderizers on Mucroprotein of Bovine Skeletal Muscle

McINTOSH

1967

Journal of Food Science

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SUMMARY— The effect of post‐mortem aging on the mucoprotein of bovine skeletal muscle was studied, and compared with the effect of papain. The effects were strikingly similar. After either treatment, the isolated mucoprotein products were observed to have lowered viscosity, various degrees of ultra‐filterability, and changes in the character of precipitates formed in the presence of alcohol or phosphotungstic acid. There was a decrease in glucosamine‐galactosamine ratio, which was indicative of lessened glucosamine content. Following post‐mortem aging, a portion of mucoprotein became extractable by KCI. This product was unfilterable, and exhibited low viscosity, with increased hexosamine content and marked loss of nitrogen. Loss of nitrogen was also observed in the ultrafilterable product which resulted after papain treatment. The mucoprotein solubilized by hot water increased in post‐mortem aging. These observations indicated that depolymerization of mucoprotein occurs as a result of either post‐mortem aging or enzyme tenderizer treatment. There appears to be a breakdown of the mucoprotein which produces fragments of lower molecular weight. Lessened nitrogen content, together with the decrease in glucosamine‐galactosamine ratio observed in the KCI‐extractable product isolated after aging as well as in the ultrafilterable product which resulted after papain treatment, indicate a splitting off of protein. Mucoprotein breakdown may be a factor in the increased tenderness as the result of either post‐mortem aging or treatment with papain‐containing tenderizers. Studies are needed which correlate mucoprotein changes with tenderness in order to establish this relationship. It is conceivable that the changes in the mucoprotein fraction observed in this study contribute significantly to the loss of integrity observed in bovine skeletal muscle after post‐mortem aging.

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Post‐Mortem Changes in Protein Extractability in Beef, Pork, and Chicken Muscle

Cited by 12 publications

References 5 publications

Mechanism of Emptying of Skeletal Muscle Cell Segments

Mechanism of Emptying of Skeletal Muscle Cell Segments

PROTEOLYTIC ACTIVITY OF Pseudomonas perolens AND EFFECTS ON PORCINE MUSCLE

Effect of Post‐Mortem Aging and Enzyme Tenderizers on Mucroprotein of Bovine Skeletal Muscle

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