Some Chemical Changes Accompanying Tenderization of Beef

McCarthy, James; King, C. G.

doi:10.1111/j.1365-2621.1942.tb17652.x

Cited by 7 publications

(2 citation statements)

References 8 publications

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“…Numerous other workers have observed increased tenderness during aging (ripening) of beef carcasses (Deatherage and Harsham, 1947;Deatherage and Reiman, 1946;Hoagland et al, 1917). It was generally accepted among early workers that this increased tenderness was due to autolysis of the muscle proteins (Bate-Smith, 1948 ;McCarthy and King, 1942), presumably by the muscle cathepsins Nikolaeva, 1936, 1942). Husaini et al (1950a,b), however, failed to find any increase in the nonprotein or proteose-peptone nitrogen fractions during aging.…”

Section: Introductionmentioning

confidence: 98%

Post‐Mortem Changes in Physical and Chemical Properties of Bovine Muscle^a

Goll

Henderson

Kline

1964

Journal of Food Science

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SUMMARY Post‐mortem changes in tenderness and protein solubility were studied in bovine semitendinosus muscles. Muscles excised immediately post‐mortem were compared with muscles left attached to the skeleton. Post‐mortem times of 0, 6, 12, 24, 72, and 312 hr were studied. Sarcoplasmic protein solubility was highest immediately after slaughter and lowest in muscles left attached to the skeleton. Myofibrillar protein solubility was decreased in muscles left attached. Protein solubility changed during the first 6 hr post‐mortem but not during the 6‐ to 312‐hr aging period. Muscles left attached to the skeleton were least tender immediately after death and gradually increased in tenderness during post‐mortem aging. Excised muscles were least tender 6–12 hr post‐mortem and became progressively more tender thereafter. Even after 312 hr of aging, excised muscles were less tender than muscles still attached to the skeleton. Protein solubility did not appear to be related to tenderness. Possible relationships of muscle contraction to tenderness were discussed.

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Section: Introductionmentioning

confidence: 98%

Post‐Mortem Changes in Physical and Chemical Properties of Bovine Muscle^a

Goll

Henderson

Kline

1964

Journal of Food Science

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“…Consequently, there were not sufficient data for statistical treatment of this sample although the difference was observed visually. McCarthy et al (1942) showed that the press juice of meat aged by the Tenderaya process (48 hr at 16°C) had a greater color density than meat aged at 2°C. However, they did not relate the color density to the protein concentration of the press juice.…”

Section: Resultsmentioning

confidence: 99%

Alterations of Bovine Sarcoplasmic Proteins as Influenced by High Temperature Aging

Thompson

Davidson

Montgomery

et al. 1968

Journal of Food Science

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SUMMARY— Effects of high temperature aging upon certain characteristics of bovine I. dorsi muscle were studied. Paired wholesale ribs of carcasses were obtained subsequent to slaughter. The left rib of each pair was held at 30°C for 24 hr, then stored at 3°C. Analogous right ribs were immediately stored at 3°C. A sampling schedule of 0, 1, 2, 3, 4, 7 and 10 days was followed. There were minor variations in moisture, pH, tyrosine‐tryptophan indices of non‐protein nitrogenous compounds and expressible moisture ratios between treatments and with time. These differences were not statistically significant. Up to three days storage, extractability of water soluble protein was greatest from muscles held at the elevated temperature. After the third day, however, extractability was greater for muscles held at 3°C. Color differences between muscles treated via the two storage temperatures were marked. Absorbance ratios (422.280 mp) of extracts showed that muscles held at the high temperature had higher extractable levels of oxymyoglobin than ribs held at 3°C. This difference remained apparent throughout the aging period. Results of DEAE‐cellulose ion exchange chromatography of the sarcoplasmic proteins showed only minor variations in profiles between the two aging treatments. Alterations did appear with time. Profile alterations did not appear related to anticipated increases in tenderness.

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