Calpain–calpastatin and toughness in M. longissimus from electrically stimulated lamb and beef carcasses

• Published in: Meat science Vol. 52; no. 1; pp. 71 - 79
• Main Authors: Morton, J.D, Bickerstaffe, R, Kent, M.P, Dransfield, E, Keeley, G.M
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01-05-1999; Elsevier
• Subjects: beef; Biological and medical sciences; cattle; cysteine proteinases; Electrical stimulation; Enzymes; Food engineering; Food industries; Fundamental and applied biological sciences. Psychology; lamb meat; lambs; Life Sciences; Meat and meat product industries; meat carcasses; meat quality; postmortem changes; proteinase inhibitors; shear strength; Temperature; tenderizing; tenderness; Texture; Toughness; Electrical stimulation; Enzymes; Toughness; Temperature; Texture; Physical dressing; Enzyme; Cysteine endopeptidases; Electrical stimulus; Meat product; Enzyme inhibitor; Calpain; Hardness; Carcass; Ripening; Peptidases; Enzymatic activity; High voltage; Quality; Hydrolases; Lamb meat; Beef; Slaughter; Tenderizing
• ISSN: 0309-1740; 1873-4138
• DOI: 10.1016/S0309-1740(98)00150-8

Shear strength, pH, temperature, μ-calpain, m-calpain and calpastatin levels were measured over a two-week post-slaughter period in
Longissimus lumborum et thoracis (LD) from six lamb and six beef carcasses. All carcasses were subjected to high voltage electrical stimulation. The toughness of the beef LD determined by a MIRINZ tenderometer at 24 h post-slaughter showed a strong correlation (
r=0.91) with pH of the LD at 3 h. Beef LD toughness at 14 days was correlated (
r=0.84) with initial m-calpain levels. In both lamb and beef, LD toughness at 4 and 14 days respectively was also correlated with initial levels of calpastatin (
r=0.85, 0.83, respectively). The strong correlation between calpastatin and the rate of tenderisation indicates that the calpain system is closely linked to the proteolytic breakdown of myofibrillar proteins. There is also evidence of an interaction between pH and μ-calpain activity. The μ-calpain, m-calpain, calpastatin, pH and temperature kinetic changes which occurred during the post-mortem ageing of beef and lamb LD were applied to a computer program which predicted rate of meat tenderisation by calculating in situ calpain activity. The closeness of fit between the predicted rate of meat tenderisation and the observed tenderness values of beef and lamb LD indicates that the post-mortem activity of μ-calpain is the major determinant of variations in tenderness. However, application of the meat tenderisation predictive program to LD from individual animals revealed that the program was not sufficiently robust for this use.