Relation of Tenderness of Beef to Aging Time at 33–35°f.

Abstract

Since the consumer demands tenderness in meat, study of beef tenderization has been a major project in our research program for several years. From time to time what seemed to be paradoxical results were obtained.Such results could be duplicated and apparently were beyond the errors expected by the testing technique which is described elsewhere by Deatherage and Reiman (1946). These apparent discrepancies were, for the most part, results contrary to the premise that tenderness increases with postmortem age of meat. If meat were a homogeneous substance one might expect that tenderness would vary directly with age, but some reflection on the heterogeneous structure of meat indicated that perhaps beef does not tenderize regularly with increasing aging time.It is impossible in this paper to review the many contributions to the knowledge of tenderness in meat. The works of Moran and Smith (1929 et seq.), Smorodintsev and co-workers (1935 et seq.), Satorius and Child (1938), Steiner (1939), Winkler (1939, Griswold and Wharton (1941), Paul, Lowe, and McClurg (1944), and Ramsbottom, Strandine, and Koonz 1945 are particularly relevant to this investigation. Up to this time, however, there has been little information available on actual tenderness changes during the process of aging meat. The lack of this information might have been due to some extent to the variability in results obtained from different tenderness-testing techniques. Since, in this laboratory, a reproducible tenderness-tasting technique has been devised and since its reliability has been evaluated to some degree, the authors felt that they might be able to estimate the relation of tenderness to post-mortem age of beef. Such information would serve a twofold purpose : (1) supply information essential for a better understanding of the nature of' tenderness in meat and ( 2 ) give data concerning the eficiency of tenderizing beef commercially by aging at 0.6-1.7"C. (33-35'F.). Accordingly this study was made of the relation between tenderness of beef and post-mortem age of beef, EXPERIMENTAL PROCEDURETwo lots of commercially slaughtered cattle were used in this investigation. The first lot consisted of 10 animals (Nos. 81, 82, 86, 87, 88, 89, 90, 95, 96, and 97). These were slaughtered the same day and their carcasses graded U. S . Good, except Nos. 86, 88, and 96 which graded U. S. Commercial. After 24 hours, both full loins from each carcass were excised and put into the 33-35°F. cooler and tested 2, 6, 10, 17, 24, 31, and 38 days

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

“…At this point, virtually all of the potentially extractable nitrogen had been extracted. These observations support the view of Deatherage and Harsham (1947) that, in beef, postmortem changes in muscle protein are completed within the first 2 weeks of aging.…”

Post‐Mortem Changes in Physical and Chemical Properties of Bovine Musclea

“…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).…”

Role of Muscle Proteinases in Maintenance of Muscle Integrity and Mass

“…The ensuing fifty years seemed to demonstrate the wisdom of Sir Hardy's dictum as scientists sought in vain for proof that roteolytic degradation was responsible for postmortem tenderization P reviewed in Go11 et al 1970;Whitaker 1959). Although meat tenderness Preaent addreas: College of Education, Tottori University, Totton 680, Japan clearly increased gradually between 1 and 14 to 17 days of storage postmortem (Deatherage and Harsham 1947; Dutson and Lawrie 1974;Go11 et al 1964; Ramsbottom and Strandine 1949), very little increase occurred during this same period in chemical measurements of proteolysis such as free amino acids (Davey and Gilbert 1966;Parrish et al 1969), free N-terminal groups (Locker 1960), or nonprotein nitrogen (Davey and Gilbert 1966;Parrish et al 1967). Indeed, it was suggested (Sharp 1963) that whatever autolysis occurred in postmortem muscle was restricted to the sarcoplasmic protein fraction, which is not directly involved in meat toughness.…”