Skip to main content

Enzymes in the meat industry

  • Chapter
Enzymes in Food Processing

Abstract

Meat has a special place in our diet and is often the most important component of a meal. Indeed, the amount spent on meat or meat products each week can be as much as a third of the household food budget. As meat is an expensive commodity, much care is generally taken in the selection of cuts or joints at the butcher’s shop or supermarket counter. However, whereas we buy our meat mainly on the basis of its appearance, the most important quality for the consumer, tenderness, can only be determined satisfactorily by eating the meat after it is cooked. Attempts so far to provide tests for such quality on carcasses or primal cuts of meat have met with limited success. In addition to the effect of growth rate, eating quality can be influenced by various factors in the slaughter operation. For example, stressful treatment of a well-finished animal pre-slaughter, or careless handling of the carcass after slaughter can produce meat that is unattractive or tough and unacceptable to the consumer. Furthermore, meat that is sold too soon after slaughter will also be of an inferior quality as the carcass needs sufficient hanging time under good storage conditions to develop full tenderness and flavour. Toughness due to poor handling or inadequate ageing is referred to as myofibrillar toughness and can be regulated to some extent.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Subscribe and save

Springer+ Basic
$34.99 /Month
  • Get 10 units per month
  • Download Article/Chapter or eBook
  • 1 Unit = 1 Article or 1 Chapter
  • Cancel anytime
Subscribe now

Buy Now

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 129.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 169.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 169.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Similar content being viewed by others

References

  • Adachi, Y., Kobayashi, N., Murachi, T. and Hatanaka, M. (1986) Ca2 +-dependent cysteine proteinase, calpains I and II are not phosphorylated in vivo. Biochem Biophys. Res. Comm., 136, 1090–1096.

    CAS  Google Scholar 

  • Adachi Y., Ishida-Takahashi, A., Takahashi, C, Takano, E., Murachi, T. and Hatanaka, M. (1991) Phosphorylation and subcellular distribution of calpastatin in human haematopoietic system cells. J. Biol. Chem. 266, 3968–3972.

    CAS  Google Scholar 

  • Alarcon-Rojo, A. and Dransfield, E. (1989) Effect of calcium ions on texture of beef during condtioning. Proceedings of the 35th International Congress of Meat Science Technology, Copenhagen, 1141–1144.

    Google Scholar 

  • Anderson, T.J. and Parrish F.C.jr (1989) Post-mortem degradation of titin and nebulin of beef steaks varying in tenderness, J. Food Sci., 54, 748–749.

    CAS  Google Scholar 

  • Anon. (1988) Enzymes Food Manufacture Ingredient and Machinery Survey, ed. Darrington, H., Morgan Grampian, London, pp. 34–36.

    Google Scholar 

  • Arnold, M.K., Parr, T, Sensky, P.L, Bardsley, R.G. and Buttery, P.J. (1995) Differential calpastatin expression in cardiac and skeletal muscle. Biochem. Soc. Trans., 23, 454S.

    Google Scholar 

  • Asghar, A. and Bhatti, A.R. (1987) Endogenous proteolytic enzymes in skeletal muscle: their significance in skeletal muscle physiology and during post-mortem ageing events in carcasses. Adv. Food Res., 31, 343–451.

    CAS  Google Scholar 

  • Azanza, J.-L., Raymond, J., Robin, J.-M., Cottin, P. and Ducastaing, A. (1979) Purification and some physico-chemical and enzymic properties of a calcium ion-activated neutral proteinase from rabbit skeletal muscle. Biochem. J., 183, 339–347.

    CAS  Google Scholar 

  • Bailey, A.J. and Etherington, D.J. (1987) Degradation of collagen. In Advances in Meat Research. Vol. 4. eds Pearson, A.M., Dutson, T.R. and Bailey, A.J., AVI, New York, pp. 305–323.

    Google Scholar 

  • Bailey, A.J. and Light, N.D. (1989) Connective Tissue in Meat and Meat Products. Elsevier Applied Science, London, pp. 195–224.

    Google Scholar 

  • Ballard, R., Bardsley, R.G. and Buttery, P.J. (1988) Changes in the activity of skeletal muscle calcium-activated neutral proteinase (EC 3.4.22.17) and its specific inhibitor in chickens grown at different rates in response to graded levels of dietary protein. Br. J. Nutr., 59, 141–147.

    CAS  Google Scholar 

  • Bandman, E. and Zdanis, D. (1988) An immunological method to assess protein degradation in postmortem muscle. Meat Sci., 22, 1–19.

    CAS  Google Scholar 

  • Bardsley, R.G., Allcock, S.M.J., Dawson, J.M., Dumelow, N.W., Lasslett, Y.V., Lockley, A.K., Parr, T. and Buttery, P.J. (1992) Effect of ß-agonists on expression of calpain and calpastatin activity in skeletal muscle. Biochimie, 74, 267–273.

    CAS  Google Scholar 

  • Barrett, A.J., Rawlings, N.D., Davies, M.E., Machleidt, W., Salveson, G. and Turk, V. (1986) Cysteine proteinase inhibitors of the cystatin superfamily. In Proteinase Inhibitors, eds Barrett, A.J. and Salveson, G., Elsevier, Amsterdam, pp. 515–569.

    Google Scholar 

  • Barrett, A.J. and Kirschke, H. (1981) Cathepsin B, cathepsin H and cathepsin L. In Methods in Enzymology, ed. Lorand, L., Academic Press, New York, pp. 535–561.

    Google Scholar 

  • Barrett, A.J. and McDonald, J.K. (1980) Endopeptidases: Mammalian Proteases, A Glossary and Bibliography, vol. 1, Academic Press, London.

    Google Scholar 

  • Béchet, D., Dransfield, E. and Ouali, A. (1993) Systematic degradation of cellular proteins: an introduction to the workshop. Biochimie, 75, 837–838.

    Google Scholar 

  • Bendall, J.R. (1973) Post-mortem changes in muscle. In The Structure and Function of Muscle, ed. Bourne, G.H., Academic Press, New York, pp. 244–309.

    Google Scholar 

  • Bendall, J.R. (1979) Muscle pH and biochemical parameters in mammalian muscles. Meat Sci., 3, 143–157.

    CAS  Google Scholar 

  • Bendall, J.R. (1980) The Electrical Stimulation of Carcasses of Meat Animals. In Developments in Meat Science, ed. Lawrie, R.A. Applied Science, Barking, pp. 37–59.

    Google Scholar 

  • Bernal, V.M. and Stanley, D.W. (1986a) Changes in the melting characteristics of bovine tendon collagen induced by a bacterial collagenase. J. Food Sci., 51, 834–835.

    CAS  Google Scholar 

  • Bernal, V.M. and Stanley, D.W. (1986b) Proteolysis of intramuscular connective tissue during post mortem conditioning of beef muscle. Proceedings of the 32nd European Meeting of Meat Research Workers, Ghent, pp. 161–164.

    Google Scholar 

  • Beuk, J.F., Savich, A.L., Goeser, P.L. and Hogan, J.M. (1962) Improvements in or relating to meat products. UK Patent, No. 913, 202.

    Google Scholar 

  • Bird, J.W.C. and Carter, J.H. (1980) Proteolytic Enzymes in Striated and Non-Striated Muscle. In Degradative Processes in Heart and Skeletal Muscle, ed. Wildenthal, K., Elsevier, Amsterdam, pp. 51–85.

    Google Scholar 

  • Bishop, M.D., Koohmaraie, M., Killefer, J. and Kappes, S. (1993) Restriction fragment length polymorphism in the bovine calpastatin gene. J. Anim. Sci., 71, 2277.

    CAS  Google Scholar 

  • Blanchard, P., Ellis, M, Maltin, G, Falkous, G, Harris, J.B. and Mantle, D. (1993) Effect of growth promoters on pig muscle structural protein and proteolytic enzyme levels in vivo and in vitro. Biochimie, 75, 839–847.

    CAS  Google Scholar 

  • Bond, J.S. and Butler, P.E. (1987) Intracellular proteases. Ann. Rev. Biochem., 56, 333–364.

    CAS  Google Scholar 

  • Bonnet, M. and Kopp, J. (1984) Dégradation du collagène musculaire de bovin par une collagénase produite par Achromobacter iophagus. Proceedings of the 30th European Meeting of Meat Research Workers, Bristol, pp. 129–130.

    Google Scholar 

  • Bouton, P.E. and Harris, P.V. (1972) The effect of some post-slaughter treatments on the mechanical properties of bovine and ovine muscles. J. Food Sci., 37, 539–543.

    Google Scholar 

  • Brocklehurst, K. (1986) Natural Structural Variation in the Cysteine Proteinases as an Aid to the Study of Mechanism by Reactivity Probe Kinetics, Catalysis Kinetics and Spectroscopic Methods. In Cysteine Proteinases and their Inhibitors, ed. Turk, V., DeGruyter, Berlin, pp. 307–325.

    Google Scholar 

  • Busch, W.A., Stromer, M.H., Goll, D.E. and Suzuki, A. (1972) Ca2+ -specific removal of Z-lines from rabbit skeletal muscle. J. Cell Biol., 52, 367.

    CAS  Google Scholar 

  • Buttle, D.J., Kembhavi, A.A., Sharp, S.L., Shute R.E., Rich, D.H. and Barrett, A.J. (1989) Affinity purification of the novel cysteine proteinase papaya proteinase IV, and papain from papaya latex. Biochem. J., 261, 469–476.

    CAS  Google Scholar 

  • Byeon, M.K., Sigi, Y., Markwald, R.R. and Hoffman, S. (1995) NCAM polypeptides in heart development:.association with Z discs of forms that contain the muscle-specific domain. J. Cell Biol., 128, 209–221.

    CAS  Google Scholar 

  • Calkins, C.R., Seideman, S.C. and Crouse, J.D. (1987) Relationships between rate of growth, catheptic enzymes and meat palatability in young bulls. J. Anim. Sci., 64, 1448–1457.

    CAS  Google Scholar 

  • Calkins, C.R. and Seideman, S.C. (1988) Relationships among calcium-dependent protease, cathepsins B and H, meat tenderness and the response of muscle to ageing. J. Anim. Sci., 66, 1186–1193.

    CAS  Google Scholar 

  • Caygill, J.C. (1979) Sulphydryl plant proteases. Enzyme Microb. Technol., 1, 233–242.

    CAS  Google Scholar 

  • Caygill, J.C. and Etherington, D.J. (1983) Fruit Bromelain and Other Plant Proteinases. In Use of Enzymes in Food Technology (Conference Proceedings), ed. Dupuy, P., Technique et Documentation Lavoisier, Paris, pp. 419–421.

    Google Scholar 

  • Chen, M.-T, Yang, W.-D. and Guo, S.-L. (1988) Differentiation between fresh beef and thawed frozen beef. Meat Sci. 24, 223–226.

    CAS  Google Scholar 

  • Coolican, S.A. and Hathaway, D.R. (1984) Effect of L-α-phosphatidylinositol on a vascular smooth-muscle Ca2+-dependent protease; reduction of the Ca2+ requirement for autolysis. J. Biol. Chem., 259, 11627–11630.

    CAS  Google Scholar 

  • Cong, J., Thompson, V.F. and Goll, D.E. (1993) Effect of monoclonal antibodies specific for the 28 kDa subunit on catalytic properties of the calpains. J. Biol. Chem., 268, 25740–25747.

    CAS  Google Scholar 

  • Croall, D.E. and Demartino, G.N. (1991) Calcium-activated neutral protease (calpain) system: structure, function and regulation. Physiol. Rev., 71, 813–847.

    CAS  Google Scholar 

  • Cronlund, A.L. and Woychik, J.H. (1987) Solubilisation of collagen in restructured beef with collagenase and α-amylase. J. Food Sci., 52, 857–860.

    CAS  Google Scholar 

  • Dahlmann, B., Kuehn, L., Ruschmann, M. and Reinauer, H. (1983) Susceptibility of musclesoluble proteins to degradation by mast cell chymase. J. Biol. Chem., 260, 12600–12606.

    Google Scholar 

  • Dahlmann, B., Kuehn, L., Heinrich, P.C., Kirschke, H. and Wiederanders, B. (1989) ATP-activated, high-molecular-mass proteinase-I from rat skeletal muscle is a cysteine proteinase-α1-macroglobulin complex. Biochim. Biophys. Acta, 991, 253–262.

    CAS  Google Scholar 

  • Davey, C.L. (1983) Post-mortem chemical changes in muscle-meat ageing. Rec. Meat Conf Proc., 36, pp. 108–115.

    Google Scholar 

  • Davey C.L. and Gilbert, K.V. (1976) The temperature coefficient of beef ageing. J. Sci. Fd. Agric., 27, 244–250.

    Google Scholar 

  • Dayton, W.R., Reville, W.J., Göll, D.E. and Stromer, M.H. (1976) A calcium-activated protease possibly involved in myofibrillar protein turnover: partial characterisation of the purified enzyme. Biochemistry, 15, 2159–2167.

    CAS  Google Scholar 

  • Dayton, W.R., Schollmeyer, J.V., Lepley, R.A. and Cortes, L.R. (1981) A calcium-activated protease possibly involved in myofibrillar protein turnover. Isolation of a low-calciumrequiring form of the protease. Biochim. Biophys. Acta, 659, 48–61.

    CAS  Google Scholar 

  • Dean, R.T. and Barrett, A.J. (1976) Lysosomes. Essays Biochem. 12, 1–39.

    CAS  Google Scholar 

  • Dransfield, E. (1986) Conditioning of Meat. In Recent Advances and Developments in the Refrigeration of Meat by Chilling. International Institute of Refrigeration, Paris, pp. 61–69.

    Google Scholar 

  • Dransfield, E. (1994) Modelling postmortem tenderisation V: inactivation of calpains. Meat Sci., 37, 391–409.

    CAS  Google Scholar 

  • Dransfield, E. and Etherington, D.J. (1981) Enzymes in the Tenderisation of Meat. In Enzymes in Food Processing, eds Birch, G.G., Blakebrough, N. and Parker, K.T., Applied Science, Barking, Essex, pp. 177–194.

    Google Scholar 

  • Ducastaing, A., Valin, C. Schollmeyer, J. and Cross, R. (1985) Effects of electrical stimulation on post-mortem changes in the activities of two Ca2 +-dependent neutral proteinases and their inhibitor in beef muscle. Meat Sci., 15, 193–202.

    CAS  Google Scholar 

  • Dufour, E., Ouali, A., Obled, A., Deval, C. and Valin, C. (1989) Lysosomal proteinase-sensitive regions in fast and slow skeletal muscle myosins. Biochimie, 71, 625–632.

    CAS  Google Scholar 

  • Dutson, T.R. (1983) Relationship of pH and temperature to disruption of specific muscle proteins and activity of lysosomal proteinases. J. Food Biochem., 7, 223–245.

    CAS  Google Scholar 

  • Edmunds, T. and Pennington, R.J.T. (1981) Mast cell origin of ‘myofibrillar protease’ of rat skeletal and heart muscle. Biochem. Biophys. Acta, 661, 28–31.

    CAS  Google Scholar 

  • Edmunds, T., Nagainis, P.A., Sathe, S.K., Thompson, V.F. and Goll, D.E. (1991) Comparison of the autolyzed and unautolyzed forms of µ- and m-calpain from bovine skeletal muscle. Biochim. Biophys. Acta, 1077, 197–208.

    CAS  Google Scholar 

  • Etherington, D.J. (1984) The contribution of proteolytic enzymes to post mortem changes in muscle. J. Anim. Sci., 59, 1644–1650.

    CAS  Google Scholar 

  • Etherington, D.J. (1987) Collagen and Meat Quality: Effects of Conditioning and Growth Rate. In Advances Meat Research Vol. 4., eds Pearson, A.M., Dutson, T.R. and Bailey, A.J. AVI, New York, pp. 351–360.

    Google Scholar 

  • Etherington, D.J. Taylor, M.A.J., and Dransfield, E. (1987) Conditioning of meat from different species: relationship between tenderising and the levels of cathepsin B, cathepsin L, calpain I, calpain II and β-glucuronidase. Meat Sci., 20, 1–18.

    CAS  Google Scholar 

  • Etherington, D.J., Taylor, M.A.J., Wakefield, D.K., Cousins, A. and Dransfield, E. (1990) Proteinase (cathepsins B, D, L, and calpains) levels and conditioning rates in normal, electrically-stimulated and high-ultimate-pH chicken muscle. Meat Sci. 28, 99–109.

    CAS  Google Scholar 

  • Etherington, D.J. and Wardale, R.J. (1982) The mononuclear cell population in rat-leg muscle: its contribution to the lysosomal enzyme activities of whole muscle extracts. J. Cell Sci., 58, 139–148.

    CAS  Google Scholar 

  • Fawcett, S.L. and McDowell, D.A. (1987) Assessment of the potential of commercially available enzymes in meat tenderisation. J. Foodservice Systems, 4, 133–142.

    Google Scholar 

  • Foegeding, E.A. and Larick, D.K. (1986) Tenderisation of beef with bacterial collagenase. Meat Sci., 18, 201–214.

    CAS  Google Scholar 

  • Fogle, D.R., Plimpton, R.F., Ockerman, H.W., Jarenback, L. and Persson, T. (1982) Tenderisation of beef: effect of enzyme, enzyme level, and cooking method. J. Food Sci., 47, 1113–1118.

    CAS  Google Scholar 

  • Forsberg, N.E., Ilian, M.A, Ali-Bar, A., Cheeke, P.R. and Wehr, N.B. (1989) Effects of cimaterol on rabbit growth and myofibrillar protein degradation and on calcium-dependent proteinase activities in skeletal muscle. J. Anim. Sci., 67, 3313–3321.

    CAS  Google Scholar 

  • Fritz, J.D., Mitchell, M.C., Marsh, B.B. and Greaser, M.L. (1993) Titin content of beef in relation to tenderness. Meat Sci., 33, 41–50.

    CAS  Google Scholar 

  • Fujii, J., Otsu, K., Zorzato, F., De Leon, S, Khanna, V.K, Weiler, J.E, O’Brien, P.J. and MacLennan, D.H. (1991) Identification of a mutation in porcine ryanodine receptor associated with malignant hyperthermia. Science, 253, 448–451.

    CAS  Google Scholar 

  • Gann, G.L. and Merkel, R.A. (1978) Ultrastructural changes in bovine longissimus muscle during post-mortem ageing. Meat Sci., 2, 129–144.

    CAS  Google Scholar 

  • Garret, C, Cottin, P, Dufourcq, J. and Ducastaing, A. (1988) Evidence for a Ca2 +-independent association between calpain II and phospholipid vesicles. FE BS Lett., 227, 20–214.

    Google Scholar 

  • Göll, D.E., Dayton, W.R, Singh, I. and Robson, R.M. (1991) Studies of the α-actinin/actin interaction in the Z-disk by using calpain. J. Biol. Chem., 266, 8501–8510.

    Google Scholar 

  • Goll, D.E., Thompson, V.F, Taylor, R.G. and Christiansen, J.A. (1992a) Role of the calpain system in muscle growth. Biochimie, 74, 225–237.

    CAS  Google Scholar 

  • Goll, D.E., Thompson, V.F, Taylor, R.G. and Zalewska, T. (1992b) Is calpain regulated by membranes and autolysis or by calcium and calpastatin? BioEssays, 14, 549–556.

    CAS  Google Scholar 

  • Gopalakrishna, R. and Barsky, S.H. (1986) Hydrophoic association of calpains with subcellular organelles. J. Biol. Chem., 261, 13936–13942.

    CAS  Google Scholar 

  • Green, R.D., Cockett, N.E, Müller, M.F, Hancock, D.L, Bidwell, CA, Barrett, L.S, Morgan, J.B. and Tatum, J.D. (1994) Characterisation of Taql polymorphisms in the bovine calpastatin gene. Proceedings of 5th World Congress on Genetics Applied to Livestock Production, 19, 450–453.

    Google Scholar 

  • Heath, R., Kay, J. Kuehn, L. Dahlmann, B. Stauber, W.T. and Mayer, M. (1987) Immunochemical characterisation of the myofibrillar proteinase from cultured rat myocytes as chymase. Biochem. Int., 14, 675–683.

    CAS  Google Scholar 

  • Higgins, J.A., Lasslett, Y.V., Bardsley, R.G. and Buttery, P.J. (1988) The relation between dietary restriction or clenbuterol (a selective β2 agonist) treatment on muscle growth and calpain proteinase (EC 3.4.22.17) and calpastatin activities in lambs. Br. J. Nutr., 60, 645–652.

    CAS  Google Scholar 

  • Hirao, T., Hara, K. and Takahashi, K, (1984) Purification and characterisation of cathepsin B from monkey skeletal muscle. J. Biochem., 95, 871–879.

    CAS  Google Scholar 

  • Ho, C.Y., Stromer, M.H. and Robson, R.M. (1994) Identification of the 30kDa polypeptide in postmortem skeletal muscle as a degradation product of Troponin-T. Biochimie, 76, 369–375.

    CAS  Google Scholar 

  • Houde, A. and Pommier, S.A. (1993) Use of the polymerase chain reaction technology to detect a mutation associated with malignant hyperthermia in different pig tissues. Meat Sci., 33, 349–358.

    CAS  Google Scholar 

  • Huang, H.-Y., Graves, D.J., Robson, R.M. and Huitt, T.W. (1993) ADP-ribosylation of the intermediate filament protein desmin and inhibition of desmin assembly in vitro by muscle ADP-ribosyltransferase. Biochem. Biophys. Res. Commun., 197, 570–577.

    CAS  Google Scholar 

  • Ilian, M.A. and Forsberg, N.E. (1994) A comparative study on gene expression of calpains, calpastatin, cathepsin D and proteasome in tissues of fed and fasted rabbits. J. Nutr. Biochem., 5, 529–535.

    CAS  Google Scholar 

  • Iversen, P., Ertbjerg, P., Larsen, L.M., Monllao, S. and Møller, A.J. (1993) An FPLC method for determination of calpains and calpastatin in porcine m longissimus dorsi. Biochimie, 75, 869–872.

    CAS  Google Scholar 

  • Jacquet, A., Kleinschmidt, T. Dubois, T., Schnek, A. G., Looze, Y. and Braunitzer, G. (1989a) The thiol proteinases from the latex of Carica papaya L, IV proteolytic specificities of chymopapain and papaya proteinase Ω determined by digestion of α-globin chains. Biol. Chem. Hoppe-Sehler, 370, 819–829.

    CAS  Google Scholar 

  • Jacquet, A., Kleinschmidt, T., Schnek, A. G., Looze, Y. and Braunitzer, G. (1989b) The thiol proteinases from the latex of Carica papaya L, III the primary structure of chymopapain. Biol. Chem. Hoppe-Sehler, 370, 425–434.

    CAS  Google Scholar 

  • Jeacocke, R.E. (1984) The kinetics of rigor onset in beef muscle fibres. Meat Sci., 11, 237–251.

    CAS  Google Scholar 

  • Johnson, P. (1990) Calpains (intracellular calcium-activated cysteine proteinases): structureactivity relationships and involvement in normal and abnormal cellular metabolism. Int. J. Biochem., 22, 811–822.

    CAS  Google Scholar 

  • Kang, C.K., Jodlowski, R.F., Donnelly, T.H. and Warner, W.D. (1982) Tenderisation of meat by natural enzyme control. US Patent, No. 4, 336, 271.

    Google Scholar 

  • Káš, J. Vánă, V. Kopečný, J. and Rauch, P. (1983) Stability of lysosomes in beef and pork muscle post-mortem. J. Lebensm. Unters. Forsch., 177, 461–467.

    Google Scholar 

  • Katunuma, N. and Kominami, E. (1987) Abnormal expression of lysosomal cysteine proteinases in muscle wasting diseases. Rev. Physiol. Biochem. Pharmacol., 108, 1–20.

    CAS  Google Scholar 

  • Kawasaki, H., Emori, Y. and Suzuki, K. (1993) Calpastatin has two distinct sites for interaction with calpain—effect of calpastatin fragments on the binding of calpain to membranes. Arch. Biochem. Biophys., 305, 467–472.

    CAS  Google Scholar 

  • Kawashima, S., Hayashi, M., Saito, Y., Kasai, Y. and Imahori, K. (1988) Tissue distribution of calcium-activated neutral proteinases in rat. Biochim. Biophys. Acta, 965, 130–135.

    CAS  Google Scholar 

  • Kay J., Heath, R., Dahlman, B., Kuehn, L. and Stauber, W.T. (1985) Serine Proteinases and Protein Breakdown in Muscle. In Intracellular Protein Catabolism, eds Khairallah, E.A., Bond, J.S. and Bird, J.W.C., A.R. Liss, New York, pp. 195–205.

    Google Scholar 

  • Kay, J., Siemankowski, L.M., Siemankowski, R.F., Greweling, J.A. and Goll, D.E. (1982) Degradation of myofibrillar proteins by a trypsin-like serine proteinase. Biochem. J., 201, 279–285.

    CAS  Google Scholar 

  • Keil, B. (1979) Some newly characterised collagenases from procaryotes and lower eucaryotes. Mol. Cell Bioch., 23, 87–108.

    CAS  Google Scholar 

  • Killefer, J. and Koohmaraie, M. (1994) Bovine skeletal muscle calpastatin: cloning, sequence analysis and steady-state mRNA expression. J. Anim. Sci., 72, 606–614.

    CAS  Google Scholar 

  • Kim, Y.S., Sainz, R.D., Summers, R.J. and Molenaar, P. (1992) Cimaterol reduces β-adrenergic receptor density in rat skeletal muscles. J. Anim. Sci., 70, 115–122.

    CAS  Google Scholar 

  • Kominami, E., Tsukahara, T., Hara, K. and Katunuma, N. (1988) Biosynthesis and processing of lysosomal cysteine proteinases in rat macrophages. FEBS Lett., 231, 225–228.

    CAS  Google Scholar 

  • Koohmaraie, M. (1992) The role of Ca2+-dependent proteases (calpains) in postmortem proteolysis and meat tenderness. Biochimie, 74, 239–245.

    CAS  Google Scholar 

  • Koohmaraie, M. (1994) Muscle proteinases and meat ageing. Meat Sci., 36, 93–104.

    CAS  Google Scholar 

  • Koohmaraie, M., Babiker, A.S., Merkel, R.A. and Dutson, T.R. (1988) Role of Ca+ +-dependent proteases and lysosomal enzymes in post-mortem changes in bovine skeletal muscle. J. Food Sci., 53, 1253–1257.

    CAS  Google Scholar 

  • Koohmaraie, M., Crouse, J.D. and Mersmann, H.T. (1989) Acceleration of post-mortem tenderisation in ovine carcasses through infusion of calcium chloride: effect of concentration and ionic strength. J. Anim. Sci., 67, 934–942.

    CAS  Google Scholar 

  • Koohmaraie, M., Schollmeyer, J.E. and Dutson, T.R. (1986) Effect of low-calcium-requiring calcium activated factor on myofibrils under varying pH and temperature conditions. J. Food. Sci., 51, 28–32.

    CAS  Google Scholar 

  • Koohmaraie, M., Seideman, S.C., Schollmeyer, J.E., Dutson, T.R. and Crouse, J.D. (1987) Effect of post-mortem storage on Ca+ +-dependent proteases, their inhibitor and myofibril fragmentation. Meat Sci., 19, 187–196.

    CAS  Google Scholar 

  • Koohmaraie, M., Whipple, G., Kretchmar, D.H., Crouse, J.D. and Mersmann, H.J. (1991) Postmortem proteolysis in longissimus muscle from beef, lamb and pork carcasses. J. Anim. Sci., 69, 617–624.

    CAS  Google Scholar 

  • Kopp, J. and Valin, C. (1980–81) Can muscle lysosomal enzymes affect muscle collagen postmortem? Meat Sci., 5, 319–322.

    Google Scholar 

  • Kretchmar, D.H., Hathaway, M.R., Epley, R.J. and Dayton, W.R. (1990) Alterations in post-mortem degradation of myofibrillar proteins in muscle of lambs fed a β-adrenergic agonist. J. Anim. Sci., 68, 1760–1772.

    CAS  Google Scholar 

  • Kuo, W.-N., Ganesan, U., Davis, D.L. and Walbey, D.L. (1994) Regulation of the phosphorylation of calpain II and its inhibitor. Molec. Cell. Biochem., 136, 157–161.

    CAS  Google Scholar 

  • Labadie, J. and Gouet, P. (1981) Nouvelle collagénase, procédé d’obtention et applications. French Patent, No. 2, 474, 052.

    Google Scholar 

  • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685.

    CAS  Google Scholar 

  • Lakey, A., Labeit, S., Gautel, M., Ferguson, C., Barlow, D.P. and Bullard, B. (1993) Kettin, a large modular protein in the Z-disc of insect muscles. EMBO J., 12, 2863–2871.

    CAS  Google Scholar 

  • Lakritz, L. and Maerker, G. (1988) Enzyme levels in raw meat after low-dose ionising radiation and extended refrigerated storage. Meat Sci., 23, 77–86.

    CAS  Google Scholar 

  • Lawrie, R.A. (1985) Meat Science 4th edn., Pergamon Press, Oxford.

    Google Scholar 

  • Lazarides, E. (1980) Intermediate filaments as mechanical integrators of cellular space. Nature, 283, 249–256.

    CAS  Google Scholar 

  • Lee, W.J., Ma, H., Takano, E., Yang, H.Q., Hatanaka, M. and Maki, M. (1992) Molecular diversity in amino terminal domains of human calpastatin by exon skipping. J. Biol. Chem., 267, 8437–8442.

    CAS  Google Scholar 

  • Lee, Y.B., Sehnert, D.J. and Ashmore, C.R. (1986) Tenderisation of meat with ginger rhizome protease. J. Food Sci., 51, 1558–1559.

    CAS  Google Scholar 

  • Lusby, M.L., Ridpath, J.F., Parrish, F.C. Jr. and Robson, R.M. (1983) Effect of post mortem storage on degradation of the myofibrillar protein titin in bovine longissimus muscle. J. Food Sci., 48, 1787–1790.

    CAS  Google Scholar 

  • Ma, H., Yang, H.Q., Takano, E., Lee, W.J., Hatanaka, M. and Maki, M. (1993) Requirement of different subdomains of calpastatin for calpain inhibition and for binding to calmodulin-like domains. J. Biochem., 113, 591–599.

    CAS  Google Scholar 

  • Ma, H., Yang, H.Q., Takano, E., Hatanaka, M. and Maki, M. (1994) Amino terminal conserved region in proteinase inhibitor domain of calpastatin potentiates its calpain inhibitory activity by interacting with calmodulin-like domain of the proteinase. J. Biol. Chem., 269, 24430–24436.

    CAS  Google Scholar 

  • Maclean, D. (1989) Beef (answer to parliamentary question). Hansard, 7 Nov., 974–978.

    Google Scholar 

  • MacDonald, J.K. and Barrett, A.J. (1986) Exopeptidases: Mammalian Proteases: a Glossary and Bibliography, Vol. 2. Academic Press, London.

    Google Scholar 

  • Makinodan, Y., Toyohara, H., Yokoyama, Y. and Kinoshita, M. (1988) The possible existence of a heat-stable alkaline proteinase (HAP) in rat skeletal muscle. Comp. Biochem. Physiol., 89B. 359–361.

    CAS  Google Scholar 

  • Mantle, D., Delday, M.I. and Maltin, C.A. (1992) Effect of clenbuterol on protease activities and protein levels in rat muscle. Muscle and Nerve, 15, 471–178.

    CAS  Google Scholar 

  • Matsukura, U., Okitani, A., Nishimuro, T. and Kato, H. (1981) Mode of degradation of myofibrillar-proteins by an endogenous proteinase, cathepsin L. Biochim. Biophys. Acta, 662, 41–47.

    CAS  Google Scholar 

  • Matsukura, J., Matsumoto, T., Tashiro, Y., Okitani, A. and Kato, H. (1984) Morphological changes in myofibrils and glycerinated muscle fibres on treatment with cathepsins D and L. Int. J. Biochem., 16, 957–962.

    CAS  Google Scholar 

  • McClelland, P. and Hathaway, D.R. (1991) The calpain-calpastatin system in vascular smooth muscle. FEBS Lett., 290, 55–57.

    CAS  Google Scholar 

  • Melloni, E. and Pontremoli, S. (1991) The calpain-calpastatin system: structural and functional properties. J. Nutr. Biochem., 2, 467.

    CAS  Google Scholar 

  • Mikami, M., Whiting, A.H., Taylor, M.A.J., Maciewicz, R.A. and Etherington D.J. (1987) Degradation of myofibrils from rabbit, chicken and beef by cathepsin L and lysosomal lysates. Meat Sci., 21, 81–97.

    CAS  Google Scholar 

  • Miller, A.J., Strange, E.D. and Whiting, R.C. (1989) Improved tenderness of restructured beef steaks by a microbial collagenase derived from Vibrio B-30. J. Food Sci., 54, 855–857.

    CAS  Google Scholar 

  • Mills, E.W., Smith, S.H., Forrest, J.C., Aberle, E.D. and Judge, M.D. (1989) Effects of early post-mortem ageing on intramuscular collagen stability, yield and composition. Meat Sci., 25, 133–141.

    CAS  Google Scholar 

  • Moeller, P.W., Fields P.A., Dutson, T.R., Landmann, W.A. and Carpenter, Z.L. (1977) High temperature effects on lysosomal enzyme distribution and fragmentation of bovine muscle. J. Food Sci., 42, 510–512.

    CAS  Google Scholar 

  • Murachi, T. (1989) Intracellular regulatory system involving calpain and calpastatin. Biochem. Int., 18, 263–294.

    CAS  Google Scholar 

  • Nagainis, P.A., Wolfe, F.H., Sathe, S.K. and Goll, D.E. (1988) Autolysis of the millimolar Ca2+-requiring form of the Ca2+-dependent proteinase from chicken skeletal muscle. Biochem. Cell Biol., 66, 1023–1031.

    CAS  Google Scholar 

  • Narushima, N. and Sekino, Y. (1988) Meat tenderisation with proteolytic enzyme-containing oil. US Patent, No. 4 725, 443.

    Google Scholar 

  • Obled, A., Ouali, A. and Valin, C. (1984) Cysteine proteinase content of rat muscle lysosomes. Evidence for an unusual proteinase activity. Biochimie, 66, 609–616.

    CAS  Google Scholar 

  • Ohno, S., Minoshima, S., Kudoh, J., Fukuyama, R., Shimizu, Y., Ohmi-Imajoh, S., Shimizu, N. and Suzuki, K. (1990) Four genes for the calpain family locate on four distinct human chromosomes. Cytogenet. Cell Genet., 53, 225–229.

    CAS  Google Scholar 

  • Okitani, A., Matsumoto, T., Kitamura, Y. and Kato, H. (1981) Purification of cathepsin D from rabbit skeletal muscle and its action towards myofibrils. Biochim. Biophys. Acta, 662, 202–209.

    CAS  Google Scholar 

  • Okitani, A., Matsuishi, M., Matsumoto, T., Kamoshida, E., Sato, M., Matsukura, U., Watanabe,. Kato, H. and Fujumaki, M. (1988) Purification and some properties of cathepsin B from rabbit skeletal muscle. Eur. J. Biochem., 177, 377–381.

    Google Scholar 

  • Okitani, A., Matsukura, U., Kato, H. and Fujimaki, M. (1980) Purification and some properties of a myofibrillar protein-degrading protease, cathepsin L, from rabbit skeletal muscle. J. Biochem., 87, 1133–1143.

    CAS  Google Scholar 

  • Okitani, A., Nishimura, T. and Kato, H. (1981) Characterisation of hydrolase H, a new muscle protease processing aminopeptidase activity. Eur. J. Biochem., 115, 269–274.

    CAS  Google Scholar 

  • Olson, D.G. and Parrish, F.C. Jr. (1977) Relationship of myofibril fragmentation index to measures of beefsteak tenderness. J. Food Sci., 42, 506–509.

    CAS  Google Scholar 

  • O’Meara, G.M. and Munro, P.A. (1984) Selection of a proteolytic enzyme to solubilise lean beef tissue. Enzyme Microb. Technol., 6, 181–185.

    Google Scholar 

  • Orcutt, M.W. and Dutson, T.R. (1985) Post-mortem degradation of gap filaments at different post-mortem pHs and temperatures. Meat Sci., 14, 221–241.

    CAS  Google Scholar 

  • Otsuka, Y., Fujita, H., Inosako, Y., Kumojima, Y., Ichimura, F., Ikemoto, E. and Kawabara, E. (1988) Characterisation of muscle low-calcium-requiring form of calcium activated protease. Agric. Biol. Chem., 52, 31–40.

    CAS  Google Scholar 

  • Ouali, A. (1984) Sensitivity of ionic strength of Mg-Ca enhanced ATPase activity as an index of myofibrillar ageing in beef. Meat Sci., 11, 79–88.

    CAS  Google Scholar 

  • Ouali, A., Garrel, N., Obled, A., Deval, C. and Valin C. (1987) Comparative action of cathepsins D, B, H, L and of a new lysosomal cysteine proteinase on rabbit myofibrils. Meat Sci., 19, 83–100.

    CAS  Google Scholar 

  • Ouali, A. and Talmant, A. (1990) Calpains and calpastatin distribution in bovine, porcine and ovine skeletal muscles. Meat Sci., 28, 331–348.

    CAS  Google Scholar 

  • Ouali, A., Zabari, M., Lacourt, A., Talmant, A., Monin, G., Kopp, J. and Valin, C. (1988) Usefulness of various biochemical and histochemical characteristics as indices of muscle type in lamb carcasses. Meat Sci., 24, 235–247.

    CAS  Google Scholar 

  • Parr, T., Bardsley, R.G., Gilmour, R.S. and Buttery, P.J. (1992) Changes in calpain and calpastatin mRNA induced by β-adrenergic stimulation of bovine skeletal muscle. Eur. J. Biochem., 208, 333–339.

    CAS  Google Scholar 

  • Penny, I.F. (1980) The Enzymology of Conditioning. In: Developments in Meat Science, ed. Lawrie, R.A., Applied Science, Barking, pp. 115–143.

    Google Scholar 

  • Penny, I.F., Etherington, D.J., Reeves, J.L. and Taylor, M.A.J. (1984) The action of cathepsin L and Ca2+-activated neutral proteases on myofibrillar proteins. Proceedings of the 30th European Meeting of Meat Research Workers, Bristol, pp. 133–134.

    Google Scholar 

  • Penny, I.F. and Ferguson-Pryce, R. (1979) Measurement of autolysis in beef muscle homogenates. Meat Sci., 3, 121–134.

    CAS  Google Scholar 

  • Penny, I.F., Taylor, M.A.J., Harris, A.G. and Etherington, D.J. (1985) Purification and immunological characterisation of two calcium-activated proteinases from rabbit skeletal muscle. Biochim. Biophys. Acta, 829, 244–252.

    CAS  Google Scholar 

  • Peter, J.B., Kar, N.C., Barnard, R.J., Pearson, C.M. and Edgerton, V.R. (1972) Distribution of acid hydrolases in guinea pig skeletal muscle. Biochem. Med., 6, 257–261.

    CAS  Google Scholar 

  • Pontremoli, S. and Melloni, E. (1986) Extralysosomal protein degradation. Ann. Rev. Biochem., 55, 455–481.

    CAS  Google Scholar 

  • Pontremoli, S., Viotti, P.L., Michetti, M., Sparatore, B., Salamino, F. and Melloni, E. (1990) Identification of an endogenous activator of calpain in rat skeletal muscle. Biochem. Biophys. Res. Commun., 171, 569–574.

    CAS  Google Scholar 

  • Pringle, T.D., Calkins, C.R., Koohmaraie, M. and Jones, S.J. (1993) Effects over time of feeding a β-adrenergic agonist to wether lambs on animal performance, muscle growth, endogenous muscle proteinase activities and meat tenderness. J. Anim. Sci., 71, 636–644.

    CAS  Google Scholar 

  • Pringle, T.D., Lonergen, S.M., Calkins, C.R., Jones, S.J., Miller, P.S. and Koohmaraie, M. (1994) Temporal response of rabbits to β-adrenergic agonist feeding, tissue weight, calpains and calpastatin activities, and nucleic acid and protein concentration. J. Anim. Sci., 72, 68–74.

    CAS  Google Scholar 

  • Rechsteiner, M., Hoffman, L. and Dubiel, W. (1993) The multicatalytic and 26S proteases. J. Biol. Chem., 268, 6065–6068.

    CAS  Google Scholar 

  • Reddy, M.K., Rabinowitz, M. and Zak, R. (1983) Stringent requirement for Ca2+ in the removal of Z-lines and α-actinin from isolated myofibrils by Ca2+-activated neutral proteinase. Biochem. J., 209, 635–641.

    CAS  Google Scholar 

  • Ritonja, A., Rowan, A.D., Buttle, D.J., Rawlings, N.D., Turk, V. and Barrett, A.J. (1989) Stem bromelain: amino-acid sequence and implication for weak binding to cystatin. FEBS Lett., 247, 419–424.

    CAS  Google Scholar 

  • Rivett, A.J. (1993) Proteasomes:multicatalytic proteinase complexes. Biochem. J., 291, 1–10.

    CAS  Google Scholar 

  • Robbins, F.M., Walker, J.E., Cohen, S.H. and Chatterjee, S. (1979) Action of proteolytic enzymes on bovine myofibrils. J. Food Sci., 44, 1672–1677.

    CAS  Google Scholar 

  • Robbins, F.M., Allen, A.L., Walker, J.E. and Cohen, S.H. (1986) Meat tenderisation with a proteolytic enzyme from Trichoderma reesei. US Patent, No. 4600589.

    Google Scholar 

  • Rolan, T.L., Davis, G.W., Seideman, S.C., Wheeler, T.L. and Miller, M.F. (1988) Effects of blade tenderisation and proteolytic enzymes on restructured steaks from beef bullock chucks. J. Food Sci., 53, 1062–1064.

    Google Scholar 

  • Saido, T.C, Shibata, M., Takenawa, T., Murofushi, H. and Suzuki, K. (1992) Positive regulation of μ-calpain by polyphosphoinositides. J. Biol. Chem., 267, 24585–24590.

    CAS  Google Scholar 

  • Salamino, F., De Tullio, R., Michetti, M., Mengotti, P., Melloni, E. and Pontremoli, S. (1994) Modulation of calpastatin specificity in rat tissues by reversible phosphorylation and dephosphorylation. Biochem. Biophys. Res. Commun., 199, 1326–1332.

    CAS  Google Scholar 

  • Samarel, A.M., Worobec, S.W., Ferguson, A.G., Decker, R.S. and Lesch, M. (1986) Limited proteolysis of rabbit cardiac procathepsin D in a cell-free system. Am. J. Physiol., 250, C589–C596.

    CAS  Google Scholar 

  • Sárraga, C., Gil, M., Arnau, J. and Montfort, J.M. (1989) Effect of curing salt and phosphate on the activity of porcine muscle proteases. Meat Sci., 25, 241–249.

    Google Scholar 

  • Saunderson, C.L. and Leslie, S. (1989) Cathepsin B, D and H activities in muscles of fast- and slow-growing strains: effect of age and diet. Comp. Biochem. Physiol., 92A, 305–311.

    CAS  Google Scholar 

  • Savell, J.W., McKeith, F.K. and Smith, G.C. (1981) Reducing post-mortem ageing time of beef with electrical stimulation. J. Food Sci., 46, 1777–1781.

    Google Scholar 

  • Schwartz, W.N. and Bird, J.W.C. (1977) Degradation of myofibrillar proteins by cathepsins B. and D. Biochem. J., 167, 811–820.

    CAS  Google Scholar 

  • Schwimmer, S. (1981) Source Book of Food Enzymology, AVI, Westport.

    Google Scholar 

  • Shackelford, S.D., Koohmaraie, M., Cundiff, L.V., Gregory, K.E., Rohrer, G.A. and Savell, J.W. (1994) Heritabilities and phenotypic and genetic correlations for bovine postrigor calpastatin activity, intramuscular fat content, Warner-Bratzler shear force, retail product yield, and growth rate. J. Anim. Sci., 12, 857–863.

    Google Scholar 

  • Small, J.V., Fürst, D.O. and Thornell, L.-E. (1992) The cytoskeletal lattice of muscle cells. Eur. J. Biochem., 208, 559–572.

    CAS  Google Scholar 

  • Sohar, I., Fekete, E., Yorke, G., Roisen, F. and Bird, J.W.C. (1987) Neutral proteinases in muscle tissue and cells. Biomed. Biochim. Acta, 46, 571–579.

    CAS  Google Scholar 

  • Sørenson, N.H. and Rasmussen, P.B. (1989) Enzymic bone cleaning and scrap meat recovery. Proceedings of the 35th International Congress on Meat Science Technology, Copenhagen, 957–962.

    Google Scholar 

  • Sorimachi, H., Imajoh-Ohmi, S., Emori, Y., Kawasaki, H., Ohno, S., Minami, Y. and Suzuki, K. (1989) Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and μ-types. J. Biol. Chem., 264, 20106–20111.

    CAS  Google Scholar 

  • Sorimachi, H., Saido, T.C. and Suzuki, K. (1994) New era of calpain research; discovery of tissue-specific calpains. FEBS Lett., 343, 1–5.

    CAS  Google Scholar 

  • Sorimachi, H., Toyama-Sorimachi, N., Saido, T.C., Kawasaki, H., Sugita, H., Miyasaka, M., Arahata, K., Ishiura, S. and Suzuki, K. (1993) Muscle-specific calpain, p94, is degraded by autolysis immediately after translation, resulting in disappearance from muscle. J. Biol. Chem., 268, 10593–10605.

    CAS  Google Scholar 

  • Speck, P.A., Collingwood, K.M., Bardsley, R.G, Tucker, G.A., Gilmour, R.S. and Buttery, P.J. (1993) Transient changes in growth and in calpain and calpastatin expression in ovine skeletal muscle after short-term dietary inclusion of cimaterol. Biochimie, 754, 917–923.

    Google Scholar 

  • Squire, J.M., Luther, P.K. and Trinick, J. (1987) Muscle Myofibril Architecture. In Fibrous Protein Structure, eds Squire, J.M. and Vibert, P.V., Academic Press, London, pp. 423–450.

    Google Scholar 

  • Stanton, C. and Light, N. (1987) The effects of conditioning on meat collagen: Part 1—evidence for gross in situ proteolysis. Meat Sci., 21, 249–265.

    CAS  Google Scholar 

  • Stanton, C. and Light, N. (1988) The effects of conditioning on meat collagen: Part 2—direct biochemical evidence for proteolytic damage in insoluble perimysial collagen after conditioning. Meat Sci., 23, 179–199.

    CAS  Google Scholar 

  • Starr, R., Almond, R.E. and Offer, G.O. (1985) Location of C-protein, H-protein and X-protein in rabbit skeletal muscle fibre types. J. Muscle Res. Cell Motil., 6, 227–256.

    CAS  Google Scholar 

  • Stauber, W.T., Fritz, V., Dahlmann, B., Gauthier, F., Kirschke, H. and Ulrich, R. (1985) Fluorescence methods for localising proteinases and proteinase inhibitors in skeletal muscle. Histochem. J., 17, 787–796.

    CAS  Google Scholar 

  • Stekolnikov, L.I., Sevastyanov, B.A., Shilov, G.G., Belousov, A.A. and Mamonov, N.D. (1981) Process for producing an enzyme preparation to tenderise meat products. US Patent, No. 4 286 062.

    Google Scholar 

  • Suzuki, K., Imajoh, S., Emori, Y., Kawasaki, H., Minami, Y. and Ohno, S. (1987) Calcium-activated neutral protease and its endogenous inhibitor: activation at the cell membrane and biological function. FEBS Lett., 220, 271–277.

    CAS  Google Scholar 

  • Suzuki, K., Imajoh, S., Emori, Y., Kawasaki, H., Minami, Y. and Ohno, S., (1988) Regulation of activity of calcium activated neutral protease. Adv. Enzymol. Rel. Areas, 21, 153–169.

    Google Scholar 

  • Suzuki, K., Tsuji, S., Kubota, S., Kimura, Y. and Imahori, K. (1981) Limited autolysis of Ca2+-activated neutral protease (CANP) changes its sensitivity to Ca2+ ions. J. Biochem., 90, 275–278.

    CAS  Google Scholar 

  • Swatland, H.J. (1980) Anisotropy and post mortem changes in the electrical resistivity and capacitance of skeletal muscle. J. Anim. Sci., 50, 67–74.

    Google Scholar 

  • Takano, E., Maki, M., Mori, H., Hatanaka, M., Marti, T., Titani, K., Kannagi, R., Ooi, T. and Murachi, T. (1988) Pig heart calpastatin: identification of repetitive domain structures and anomalous behaviour in Polyacrylamide gel electrophoresis. Biochemistry, 27, 1964–1972.

    CAS  Google Scholar 

  • Takano, E., Nosaka, T., Lee, W.J., Nakamura, T., Takahashi, T., Funaki, M., Okada, H., Hatanaka, M. and Maki, M. (1993) Molecular diversity of calpastatin in human erythroid cells. Arch. Biochem. Biophys., 303, 349–354.

    CAS  Google Scholar 

  • Taylor, M.A.J., and Etherington, D.J. (1991) The solubilisation of myofibrillar proteins by calcium ions. Meat Sci., 29, 211–219.

    CAS  Google Scholar 

  • Toldrá, F. and Etherington, D.J. (1988) Examination of cathepsins B, D, H and L activities in dry-cured hams. Meat Sci., 23, 1–7.

    Google Scholar 

  • Towatari, T. and Katunuma, N. (1988) Amino acid sequence of rat liver cathepsin L. FEBS Lett., 236, 57–61.

    CAS  Google Scholar 

  • Towbin, H., Staehelin, T. and Gordon, J. (1979) Electrophoretic transfer of proteins from Polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci., 76, 4350–4354.

    CAS  Google Scholar 

  • Trinick, J. (1991) Elastic filaments and giant proteins in muscle. Curr. Opin. Cell Biol., 3, 112–119.

    CAS  Google Scholar 

  • Trinick, J. (1994) Titin and nebulin: protein rulers in muscle? Trends in Biochem. Sci., 19, 405–409.

    CAS  Google Scholar 

  • Troy, D.J., Tarrant, V.P. and Harrington, M.G. (1986) Electrophoretic analysis of changes in beef myofibrillar proteins during the early post-mortem period. Biochem. Soc. Trans., 14, 436–438.

    CAS  Google Scholar 

  • Troy, D.J. and Tarrant, V.P. (1987a) Changes in myofibrillar proteins from electrically stimulated beef. Biochem. Soc. Trans., 15, 279–298.

    Google Scholar 

  • Troy, D.J., Tarrant, V.P., and Harrington, M.G. (1987b) Changes in myofibrils during conditioning of high pH beef. Biochem. Soc. Trans., 15, 299–300.

    CAS  Google Scholar 

  • Vanderslice, P., Craik, C.S., Nadel, J. A. and Caughey, G.H. (1989) Molecular cloning of dog mast-cell tryptase and a related protease: structural evidence of a unique mode of serine proteinase activation. Biochemistry, 28, 4148–4155.

    CAS  Google Scholar 

  • Vidalenc, P., Cottin, P., Merdaci, N. and Ducastaing, A. (1983) Stability of two Ca2+-dependent neutral proteinases and their specific inhibitor during post-mortem storage of rabbit skeletal muscle. J. Sci. Food Agric., 34, 1241–1250.

    CAS  Google Scholar 

  • Vignon, X., Beaulaton, J. and Ouali, A. (1989) Ultrastructural localisation of calcium in post-mortem bovine muscle: a cytochemical and X-ray microanalytical study. Histochem. J., 21, 403–411.

    CAS  Google Scholar 

  • Vollmer, A.N. and Rosenfield, R.G. (1983) Extraction of protein from pork bones. US Patent No. 4 402 873.

    Google Scholar 

  • Voyle, C.A. (1981) Scanning electron microscopy in meat science. Scanning Electron Microscopy, 3, 405–413.

    Google Scholar 

  • Wang, S.-Y. and Beermann, D.H. (1988) Reduced calcium-dependent proteinase activity in cimaterol-induced muscle hypertrophy in lambs. J. Anim. Sci., 66, 2545–2550.

    CAS  Google Scholar 

  • Warner, W.D., Kang, C.K. and Rice, E.E. (1976) Tenderisation of meat with proteolytic enzymes. UK Patent. No. 1 448 498.

    Google Scholar 

  • Weber, M.M. (1971) Method of tenderising meat. US Patent. No. 3 561 976.

    Google Scholar 

  • Whipple, G. and Koohmaraie, M. (1993) Calcium chloride marination effects on beef steak tenderness and calpain proteolytic activity. Meat Sci., 33, 265–275.

    CAS  Google Scholar 

  • White, T.J., Meade, J.H., Shoemaker, S.P., Koths, K.E. and Innis, M.A. (1984) Enzyme cloning for the food fermentation industry. Food Technol., 38(2), 90–98.

    CAS  Google Scholar 

  • Wieland, H. (1972) Enzymes in Food Processing and Products, Noyes Data Corp., New Jersey, pp. 130–164.

    Google Scholar 

  • Willadsen, K.A., Butters, C.A., Hill, L.E. and Tobacman, L.S. (1992) Effects of the amino terminal regions of tropomyosin and troponin T on thin filament assembly. J. Biol. Chem., 267, 23746–23752.

    CAS  Google Scholar 

  • Wismer-Pederson, J. and Weber, A. (1987) Immunochemical index for beef ageing. Fleischwirtsch., 67, 351–355.

    Google Scholar 

  • Wolfe, F.H., Sathe, S.K., Goll, D.E., Kleese, W.C., Edmunds, T. and Duperret, S.M. (1989) Chicken skeletal muscle has three Ca2+-dependent proteinases. Biochim. Biophys. Acta, 998, 236–250.

    CAS  Google Scholar 

  • Wood, L., Bird, J.W.C., Yorke, G. and Roisen, F.J. (1986) Chicken and rat muscle cystatins and their localisation in cultured myoblasts. In Cysteine Proteinases and Their Inhibitors, ed. Turk, V., DeGruyter, Berlin, 667–683.

    Google Scholar 

  • Wu, F.Y., Dutson, T.R., Valin, C., Cross, H.R. and Smith, S.B. (1985) Ageing index, lysosomal enzyme activities, and meat tenderness in muscles from electrically stimulated bull and steer carcasses. J. Food. Sci., 50, 1025–1028.

    CAS  Google Scholar 

  • Wu, J.J., Dutson, T.R. and Carpenter, Z.L. (1981) Effect of post-mortem time and temperature on the release of lysosomal enzymes and their possible effect on bovine connective tissue components of muscles. J. Food Sci., 46, 1132–1135.

    CAS  Google Scholar 

  • Wu, J.J., Dutson, T.R. Carpenter, Z.L. (1982) Effect of post mortem time and temperature on bovine intramuscular collagen. Meat Sci., 7, 161–168.

    CAS  Google Scholar 

  • Wu, L.P. and Lee, Y.B. (1986) Effect of post mortem pH and temperature on bovine muscle structure and meat tenderness, J. Food. Sci., 51, 774–780.

    Google Scholar 

  • Young, O.A., Graafhuis, A.E. and Davey, C.L. (1981) Post mortem changes in cytoskeletal proteins of muscle. Meat Sci., 5, 41.

    Google Scholar 

  • Zeece, M.G. and Katoh, K. (1989) Cathepsin D and its effects on myofibrillar proteins: a review. J. Food Biochem., 13, 157–178.

    CAS  Google Scholar 

  • Zeece, M.G., Robson, R.M., Lusby, M.L. and Parrish, F.C. jr. (1986) Effect of calcium activated protease (CAF) on bovine myofibrils under different conditions of pH and temperature. J. Food Sci., 51, 797–803.

    CAS  Google Scholar 

  • Zimmerman, U.-J.P. and Schlaepfer, W.W. (1984) Multiple forms of Ca-activated proteasefrom rat brain and muscle. J. Biol. Chem., 259, 3210–3218.

    CAS  Google Scholar 

Download references

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1995 Springer Science+Business Media Dordrecht

About this chapter

Cite this chapter

Etherington, D.J., Bardsley, R.G. (1995). Enzymes in the meat industry. In: Tucker, G.A., Woods, L.F.J. (eds) Enzymes in Food Processing. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2147-1_5

Download citation

  • DOI: https://doi.org/10.1007/978-1-4615-2147-1_5

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-5897-8

  • Online ISBN: 978-1-4615-2147-1

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics