Alterations of Bovine Sarcoplasmic Proteins as Influenced by High Temperature Aging

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Abstract
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.