Hostname: page-component-586b7cd67f-t8hqh Total loading time: 0 Render date: 2024-11-26T21:57:49.992Z Has data issue: false hasContentIssue false
  • English
  • Français

Determinants of meat quality: tenderness

Published online by Cambridge University Press:  05 March 2007

Charlotte Maltin ,
Denis Balcerzak ,
Rachel Tilley  and
Margaret Delday
Charlotte Maltin*
Affiliation:
Muscle Biology Group, Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen, AB21 9SB, UK
Denis Balcerzak
Affiliation:
Muscle Biology Group, Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen, AB21 9SB, UK
Rachel Tilley
Affiliation:
Muscle Biology Group, Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen, AB21 9SB, UK
Margaret Delday
Affiliation:
Muscle Biology Group, Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen, AB21 9SB, UK
*
*Corresponding author: Dr Charlotte Maltin, fax +44 1224 716687, [email protected]
Rights & Permissions [Opens in a new window]

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

Meat quality is a term used to describe a range of attributes of meat. Consumer research suggests that tenderness is a very important element of eating quality and that variations in tenderness affect the decision to repurchase. The present paper highlights recent information on the factors that affect tenderness. While the precise aetiology is not fully understood, a number of factors have been shown to affect tenderness. Of these factors, postmortem factors, particularly temperature, sarcomere length and proteolysis, which affect the conversion of muscle to meat, appear most important. However, it is now becoming clear that variation in other factors such as the muscle fibre type composition and the buffering capacity of the muscle together with the breed and nutritional status of the animals may also contribute to the observed variation in meat tenderness.

Keywords

Meat qualityTendernessPostmortem factorsMuscle fibre characteristics
Type
Animal Nutrition and Metabolism Group Symposium on ‘Fatty acids, forages and food quality’
Information
Proceedings of the Nutrition Society , Volume 62 , Issue 2 , May 2003 , pp. 337 - 347
Copyright
Copyright © The Nutrition Society 2003

References

Abe, A (2000) Review: Role of histidine-related compounds as intracellular proton buffering constituents in vertebrate muscle. Biochemistry 65, 757–765.Google ScholarPubMed
Aberle, ED, Reeves, ES, Judge, MD, Hunsley, RE & Perry, TW (1981) Palatability and muscle characteristics of cattle with controlled weight gain: time on a high energy diet. Journal of Animal Science 52, 757–763.CrossRefGoogle Scholar
Allingham, PG, Harper, GS, Hennessy, DW & Oddy, VH (2001) The influence of pre-weaning nutrition on biochemical and myofibre characteristics of bovine semitendinosus muscle. Australian Journal of Agricultural Research 52, 891–902.CrossRefGoogle Scholar
Bader, VR (1983) Vergleichende histometrische und histologische Untersuchungen an der Skelettmuskulatur von Wild- und Hausschweinen (Comparative histometric and histological examination of the skeletal muscle of wild and domesticated pigs). Berliner und Munchener. Tierarztliche Wochenschrift 96, 89–97.Google Scholar
Balcerzak, D, Querengesser, L, Dixon, WT & Baracos, VE (2001) Coordinate expression of matrix-degrading proteinases and their activators and inhibitors in bovine skeletal muscle. Journal of Animal Science 79, 94–107.CrossRefGoogle ScholarPubMed
Bardsley, RG, Allcock, SM, Dawson, JM, Dumelow, NW, Higgins, JA, Lasslett, YV, Lockley, AK, Parr, T & Buttery, PJ (1992) Effect of beta-agonists on expression of calpain and calpastatin activity in skeletal muscle. Biochimie 74, 267–273.CrossRefGoogle ScholarPubMed
Bee, G, Solomon, MB, Czerwinski, SM, Long, C & Pursel, VG (1999) Correlation between histochemically assessed fibre type distribution and isomyosin and myosin heavy chain content in porcine skeletal muscles. Journal of Animal Science 77, 2104–2111.CrossRefGoogle ScholarPubMed
Bindon, BM & Jones, NM (2001) Cattle supply, production systems and markets for Australian beef. Australian Journal of Experimental Agriculture 41, 861–877.CrossRefGoogle Scholar
Blanchard, PJ (1994) The influence of lean tissue growth rate on pork tenderness. Meat Focus International November issue, 457–458.Google Scholar
Blanchard, PJ, Ellis, M, Warkup, CC, Hardy, B, Chadwick, JP & Deans, GA (1999a) The influence of rate of lean and fat tissue development on pork eating quality. Animal Science 68, 477–485.CrossRefGoogle Scholar
Blanchard, PJ, Warkup, CC, Ellis, M, Willis, MB & Avery, P (1999b) The influence of the proportion of Duroc genes on growth, carcass and pork eating quality characteristics. Animal Science 68, 495–501.CrossRefGoogle Scholar
Boehm, ML, Kendall, TL, Thompson, VF & Goll, DE (1998) Changes in the calpains and calpastatin during postmortem storage of bovine muscle. Journal of Animal Science 76, 2415–2434.CrossRefGoogle ScholarPubMed
Boldyrev, AA & Severin, SE (1990) The histidine-containing dipeptides, carnosine and anserine: distribution, properties and biological significance. Advances in Enzyme Regulation 30, 175–194.CrossRefGoogle ScholarPubMed
Boleman, SJ, Boleman, SL, Miller, RK, Taylor, JF, Cross, HR, Wheeler, TL, Koohmaraie, M, Shackelford, SD, Miller, MF, West, RL, Johnson, DD & Savell, JW (1997) Consumer evaluation of beef of known categories of tenderness. Journal of Animal Science 75, 1521–1524.CrossRefGoogle ScholarPubMed
Brocks, L, Klont, RE, Buist, W, de, Greef, K, Tieman, M, Engel B (2000) The effects of selection of pigs on growth rate vs leanness on histochemical characteristics of different muscles. Journal of Animal Science 78, 1247–1254.CrossRefGoogle ScholarPubMed
Bruce, HL & Ball, RO (1990) Postmortem interactions of muscle temperature, pH and extension on beef quality. Journal of Animal Science 68, 467–475.CrossRefGoogle ScholarPubMed
Čandek-Potokar, M, Žlender, B & Bonneau, M (1998) Effects of breed and slaughter weight on longissimus muscle biochemical traits and sensory quality in pigs. Annales de Zootechnie 47, 3–16.CrossRefGoogle Scholar
Ciobanu, D, Bastiaansen, J, Malek, M, Helm, J, Woollard, J, Plastow, G & Rothschild, M (2001) Evidence for new alleles in the protein kinase adenosine monophosphate-activated gamma(3)-subunit gene associated with low glycogen content in pig skeletal muscle and improved meat quality. Genetics 159, 1151–1162.CrossRefGoogle ScholarPubMed
Cottin, P, Thompson, VF, Saithe, SK, Szpancenko, A & Goll, DE (2001) Autolysis of μ- and m-calpain from bovine skeletal muscle. Biological Chemistry 382, 767–776.CrossRefGoogle ScholarPubMed
Delgado, EF, Geesink, GH, Marchello, JA, Goll, DE & Koohmaraie, M (2001) Properties of myofibril-bound calpain activity in longissimus muscle of callipyge and normal sheep. Journal of Animal Science 79, 2097–2107.CrossRefGoogle ScholarPubMed
Devine, CE, Wahlgren, NM & Tornberg, E (1999) Effect of rigor temperature on muscle shortening and tenderisation of restrained and unrestrained beef m-longissimus thoracis et lumborum. Meat Science 51, 61–72.CrossRefGoogle Scholar
Doumit, ME & Koohmaraie, M (1999) Immunoblot analysis of calpastatin degradation: Evidence for cleavage by calpain in post mortem muscle. Journal of Animal Science 11, 1467–1473.CrossRefGoogle Scholar
Dransfield, E (1981) Eating quality of DFD beef. Current Topics in Veterinary Medicine and Animal Science 10, 344–361.Google Scholar
Duckett, SK, Snowder, GD & Cockett, NE (2000) Effect of the callipyge gene on muscle growth, calpastatin activity, and tenderness of three muscles across the growth curve. Journal of Animal Science 78, 2836–2841.CrossRefGoogle ScholarPubMed
Ellis, M, Webb, AJ, Avery, PJ & Brown, I (1996) The influence of terminal sire genotype, sex, slaughter weight, feeding regime and slaughter-house on growth performance and carcass and meat quality in pigs and on the organoleptic properties of fresh pork. Animal Science 62, 521–530.CrossRefGoogle Scholar
Essén-Gustavsson, B (1992) Muscle-fibre characteristics in pigs and relationships to meat-quality parameters – review Pork Quality: Genetic and Metabolic Factors 140–157 Puolanne E Derneyer DI Ruusunen M Ellis S Wallingford, Oxon CAB International.Google Scholar
Essén-Gustavsson, B & Lindholm, A (1984) Fiber types and meta- bolic characteristics in muscles of wild boars, normal and halothane sensitive Swedish Landrace pigs. Comparative Biochemistry and Physiology 78, 67–71.CrossRefGoogle Scholar
Fang, S-H, Nishimura, T & Takahashi, K (1999) Relationship between development of intramuscular connective tissue and toughness of pork during growth of pigs. Journal of Animal Science 77, 120–130.CrossRefGoogle ScholarPubMed
Ferguson, DM, Bruce, HL, Thompson, JM, Egan, AF, Perry, D & Shorthose, WR (2001) Factors affecting beef palatability – farm gate to chilled carcass. Australian Journal of Experimental Agriculture 41, 879–891.CrossRefGoogle Scholar
Fiedler, I, Rehefeldt, C, Albrecht, E & Henning, M (1998) Histo- physiological features of skeletal muscle and adrenal glands in wild-type and domestic pigs during growth (short communication). Archiv fur Tierzucht 41, 489–495.Google Scholar
Freking, BA, Keele, JW, Shackelford, SD, Wheeler, TL, Koohmaraie, M, Nielsen, MK & Leymaster, KA (1999) Evaluation of the ovine callipyge locus: III. Genotypic effects on meat quality traits. Journal of Animal Science 77, 2336–2344.CrossRefGoogle ScholarPubMed
Garlick, PJ, Maltin, CA, Baillie, AG, Delday, MI & Grubb, DA (1989) Fiber-type composition of nine rat muscles. II. Relationship to protein turnover. American Journal of Physiology 257 E828 – E832.Google ScholarPubMed
Geesink, GH, Bekhit, AD & Bickerstaffe, R (2000) Rigor temper- ature and meat quality characteristics of lamb longissimus muscle. Journal of Animal Science 78, 2842–2848.CrossRefGoogle Scholar
Goll, DE (2000) The Calpain family of proteases. http://ag.arizona.edu/calpains/.Google Scholar
Goll, DE, Thompson, VE, Taylor, RG & Zalewska, T (1992) Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin?. BioEssays 14, 549–556.CrossRefGoogle ScholarPubMed
Henckel, P, Oksbjerg, N, Erlandsen, E, Barton-Gade, P & Bejerholm, C (1997) Histo- and biochemical characterization of the Longissimus dorsi muscle in pigs and their relationship to performance and meat quality. Meat Science 47, 311–321.CrossRefGoogle Scholar
Hornick, JL, Van, Eenaeme, C, Clinquart, A, Diez, M, Istasse L (1998) Different periods of feed restriction before compensatory growth in Belgian Blue Bulls. I. Animal performance, nitrogen balance, meat characteristics and fat composition. Animal Science 69, 563–572.CrossRefGoogle Scholar
Ilian, MA, Morton, JD, Kent, MP, Le, Couteur, CE, Hickford, J, Cowley, R Bickerstaffe, R (2001) Intermuscular variation in tenderness: Association with the ubiquitous and muscle-specific calpains. Journal of Animal Science 79, 122–132.CrossRefGoogle ScholarPubMed
Jeacocke, RE (1993) The concentration of free magnesium and calcium ions both increase in muscle fibres entering rigor mortis. Meat Science 35, 27–45.CrossRefGoogle ScholarPubMed
Jones, SW, Parr, T, Sensky, PL, Scothern, GP, Bardsley, RG & Buttery, PJ (1999) Fibre type-specific expression of p94, a skeletal muscle-specific calpain. Journal of Muscle Research and Cell Motility 20, 417–424.CrossRefGoogle ScholarPubMed
Kanawa, R, Ji, JR & Takashashi, K (2002) Inactivity of mu-calpain throughout postmortem aging of meat. Journal of Animal Science 67, 635–638.Google Scholar
Karlsson, A, Enfalt, AC, Essen-Gustavsson, B, Lundstrom, K, Rydhumer, L & Stern, S (1993) Muscle histochemical and biochemical properties in relation to meat quality during selection for increased lean tissue growth rate in pigs. Journal of Animal Science 71, 930–938.CrossRefGoogle ScholarPubMed
Karlsson, AH, Klont, RE & Fernandez, X (1999) Skeletal muscle fibres as factors for pork quality. Livestock Production Science 60, 255–269.CrossRefGoogle Scholar
Klont, RE, Brocks, L & Eikelenboom, G (1998) Muscle fibre type and meat quality. Meat Science 49, 219–229.CrossRefGoogle Scholar
Koch, RM, Jung, HG, Crouse, JD, Varel, VH & Cundiff, LV (1995) Growth, digestive capability, carcass, and meat characteristics of Bison bison, Bos taurus, and Bos×Bison. Journal of Animal Science 73, 1271–1281.CrossRefGoogle Scholar
Koohmaraie, M (1992) The role of Ca(2+)-dependent proteases (calpains) in postmortem proteolysis and meat tenderness. Biochimie 74, 239–245.CrossRefGoogle ScholarPubMed
Koohmaraie, M (1996) Biochemical factors regulating the tough- ening and tenderization processes of meat. Meat Science 43 Suppl. S193–S201.CrossRefGoogle Scholar
Koohmaraie, M, Shackelford, SD, Wheeler, TL, Lonergan, SM & Doumit, ME (1995) A muscle hypertrophy condition in lamb (Callipyge): Characterization of effects on muscle growth and meat quality traits. Journal of Animal Science 73, 3596–3607.CrossRefGoogle ScholarPubMed
Koohmaraie, M, Whipple, G, Kretchmar, DH, Crosue, JD & Mersmann, HJ (1991) Post mortem proteolysis in longissimus muscle from beef lamb and pork carcasses. Journal of Animal Science 69, 617–624.CrossRefGoogle Scholar
Kristensen, L & Purslow, PP (2001) The effect of ageing on the water holding capacity of pork: role of cytoskeletal proteins. Meat Science 58, 17–23.CrossRefGoogle ScholarPubMed
Lebret, B, Le, Roy, P, Monin, G, Lefaucheur, L, Caritez, JC, Talmanat, A, Elsen, JM, Sellier P (1999) Influence of the three RN genotypes on chemical composition, enzyme activities, and myofibre characteristics of porcine skeletal muscle. Journal of Animal Science 77, 1482–1489.CrossRefGoogle Scholar
Lefaucheur, L, Ecolan, P, Plantard, L & Gueguen, N (2002) New insights into muscle fibre types in the pig. Journal of Histo- chemistry and Cytochemistry 50, 719–730.CrossRefGoogle ScholarPubMed
Leheska, JM, Wulf, DM, Clapper, JA, Thaler, RC & Maddock, RJ (2002) Effects of high-protein/low-carbohydrate swine diets during the final finishing phase on pork muscle quality. Journal of Animal Science 80, 137–142.CrossRefGoogle ScholarPubMed
Lobley, GE (1998) Nutritional and hormonal control of muscle and peripheral tissue metabolism in farm species. Livestock Production Science 56, 91–114.CrossRefGoogle Scholar
Lobley, GE, Sinclair, KD, Grant, CM, Miller, L, Mantle, D, Calder, AG, Warkup, CC & Maltin, CA (2000) The effects of breed and level of nutrition on whole-body and muscle protein metabolism in pure-bred Aberdeen Angus and Charolais beef steers. British Journal of Nutrition 84, 275–284.CrossRefGoogle ScholarPubMed
Lonergan, SM, Huff-Lonergan, E, Rowe, LJ, Kuhlers, DL & Jungst, SB (2001) Selection for lean growth efficiency in Duroc pigs influences pork quality. Journal of Animal Science 79, 2075–2085.CrossRefGoogle ScholarPubMed
Lorenzen, CL, Koohmaraie, M, Shackelford, SD, Jahoor, F, Freetly, HC, Wheeler, TL, Savell, JW & Fiorotto, ML (2000) Protein kinetics in callipyge lambs. Journal of Animal Science 78, 78–87.CrossRefGoogle ScholarPubMed
Lundstrom, K, Anderson, A & Hanson, I (1996) Effect of the RN gene on technological and sensory meat quality in crossbred pigs with Hampshire as terminal sire. Meat Science 42, 145–153.CrossRefGoogle ScholarPubMed
McDonagh, MB, Fernandez, C & Oddy, VH (1999) Hind-limb protein metabolism and calpain system activity influence post- mortem change in meat quality in lamb. Meat Science 52, 9–18.CrossRefGoogle ScholarPubMed
McPherron, AC, Lee, S-J (1997) Double muscling in cattle due to mutations in the myostatin gene. Proceedings of the National Academy of Science USA 94, 12457–12461.CrossRefGoogle ScholarPubMed
McPherron, AC, Lee, S-J (2002) Suppression of body fat accumulaiton in myostatin-deficient mice. Journal of Clinical Investigation 109, 595–601.CrossRefGoogle Scholar
Maddock, RJ, Bidner, BS, Carr, SN, McKeith, FK, Berg, EP & Savell, JW (2002) Creatine monohydrate supplementation and quality of fresh pork in normal and halothane carrier pigs. Journal of Animal Science 80, 997–1004.CrossRefGoogle ScholarPubMed
Maltin, CA, Delday, MI, Sinclair, KD, Steven, J & Sneddon, AA (2001a) Impact of manipulations of myogensis in utero on the performance of adult skeletal muscle. Reproduction 122, 359–374.CrossRefGoogle Scholar
Maltin, CA, Lobley, GE, Grant, CM, Miller, LA, Kyle, DJ, Horgan, GW, Matthews, KR & Sinclair, KD (2001b) Factors influencing beef eating quality. 2. Effects of nutritional regimen and genotype on muscle fibre characteristics. Animal Science 72, 279–287.CrossRefGoogle Scholar
Maltin, CA, Sinclair, KD, Warriss, PD, Grant, CM, Porter, AD, Delday, MI & Warkup, CC (1998a) The effect of age at slaughter, genotype and finishing system on the biochemical properties, muscle fibre type characteristics and eating quality of bull beef from suckled calves. Animal Science 66, 341–348.CrossRefGoogle Scholar
Maltin, CA, Steven, JS & & Warkup, CC (1998b) Assay for Duroc Muscle Fibre Type. International Application Published under the Patent Cooperation Treaty. International Publication no. WO 98/15837 16 April 1998.Google Scholar
Maltin, CA, Warkup, CC, Matthews, KR, Grant, CM, Porter, AD & Delday, MI (1997) Pig muscle fibre characteristics as a source of variation in eating quality. Meat Science 47, 237–248.CrossRefGoogle ScholarPubMed
Marsh, BB, Ringkob, TP, Russell, RL, Swartz, DR & & Pagel, LA (1988) Mechanisms and strategies for improving meat tenderness. Reciprocal Meat Conference Proceedings 41, 113–118.Google Scholar
Meat and Commission (1991) A Blueprint for Improved Consistent Quality Beef Milton Keynes Meat and Livestock Commission.Google Scholar
Meat and Commission (1993) A Blueprint for Lean and Tender Pork Milton Keynes Meat and Livestock Commission.Google Scholar
Meat and Commission (1995) A Blueprint for Lean and Tender British Lamb Milton Keynes Meat and Livestock Commission.Google Scholar
Moloney, AP, Mooney, MT, Kerry, JP & Troy, DJ (2001) Producing tender and flavoursome beef with enhanced nutritional characteristics. Proceedings of the Nutrition Society 60, 221–229.CrossRefGoogle ScholarPubMed
Monin, G, Larzul, C, Le, Roy, P, Culioli, J, Mourot, J, Rousset-Akrim, S, Talmant, A, Touraille, C, Sellier P (1999) Effects of Halothane genotype and slaughter weight on texture of pork. Journal of Animal Science 77, 408–415.CrossRefGoogle ScholarPubMed
Morrison, EH, Mielche, MM Purslow (1998) Immunolocalization of intermediate filaments in porcine meat. Fibre type and muscle specific variations during conditioning. Meat Science 50, 91–104.CrossRefGoogle Scholar
Murray, RD, Cartwright, TA, Downham, DY, Murray, MA, de, Kruif A (2002) Comparison of external and internal pelvic measurements of Belgian Blue cattle from sample herds in Belgium and the United Kingdom. Reproduction in Domestic Animals 37, 1–7.CrossRefGoogle ScholarPubMed
Ockerman, HW, Jaworek, D, VanStavern, B, Parrett, N & Pierson, CJ (1984) Castration and sire effects on carcase traits, meat palatability and muscle fibre characteristics in Angus cattle. Journal of Animal Science 59, 981–990.CrossRefGoogle Scholar
Oddy, VH (1999) Protein metabolism and nutrition in farm animals: an overview Protein Metabolism and Nutrition. European Association for Animal Production Publication no. 96, 9–23 [Lobley, GE,White, A and MacRae, JC, editor]. Wageningen: Wageningen Pers.Google Scholar
Oddy, VH, Harper, GS, Greenwood, PL & McDonagh, MB (2001) Nutritional and developmental effects on the intrinsic properties of muscles as they relate to the eating quality of beef. Australian Journal of Experimental Agriculture 41, 921–942.CrossRefGoogle Scholar
Oksbjerg, N, Petersen, JS, Sørensen, IL, Henckel, P, Vestergaard, M, Ertbjerg, P, Møller, AJ, Bejerholm, C, Støier, S (2000) Long-term changes in performance and meat quality of Danish Landrace pigs: a study on a current compared with an unimproved genotype. Animal Science 71, 81–92.CrossRefGoogle Scholar
Oksbjerg, N, Sorensen, MT & Vestergaard, M (2002) Compensatory growth and its effect on muscularity and technological meat quality in growing pigs. Acta Agriculturae Scandinavica 52, 85–90.CrossRefGoogle Scholar
O'Quinn, PR, Andrews, BS, Goodbrans, RD, Unruh, JA, Nelssen, JL, Woodworth, JC, Tokach, MD & Owen, KQ (2000) Effects of modified tall oil and creatine monohydrate on growth performance, carcass characteristics & meat quality of growing–finishing pigs. Journal of Animal Science 78, 2376–2382.CrossRefGoogle ScholarPubMed
Parr, T, Sensky, PL, Scothern, GP, Bardsley, RG, Buttery, PJ, Wood, JD & Warkup, C (1999) Relationship between skeletal muscle- specific calpain and tenderness of conditioned porcine longissimus muscle. Journal of Animal Science 77, 661–668.CrossRefGoogle ScholarPubMed
Parrish, FC, Selvig, CJ, Culler, JR & Zeece, MG (1981) CAF activation, calcium concentration and the 30,000 dalton component of tough and tender bovine longissimus muscle. Journal of Food Science 46, 308–309.CrossRefGoogle Scholar
Rahelic, S & Puac, S (1981) Fibre types in Longissmus dorsi from wild and highly selected pig breeds. Meat Science 5, 439–450.CrossRefGoogle Scholar
Robins, SP, Shimokamaki, S & Bailey, AJ (1973) The chemistry of the collagen cross-links. Age related changes in the reducible components of intact collagen fibres. Biochemical Journal 131, 771–780.CrossRefGoogle ScholarPubMed
Rosenvold, K, Petersen, JS, Laerke, HN, Jensen, SK, Therkildsen, M, Karlsson, AH, Møller, HS & Andersen, HJ (2001) Muscle glycogen stores and meat quality as affected by strategic finishing feeding of slaughter pigs. Journal of Animal Science 79, 382–391.CrossRefGoogle ScholarPubMed
Scanga, JA, Belk, KE, Tatum, JD & Smith, GC (2001) Supra- nutritional oral supplementation with vitamin D 3 and calcium and the effects on beef tenderness. Journal of Animal Science 79, 912–918.CrossRefGoogle Scholar
Sensky, PL, Parr, T, Lockley, AK, Bardsley, RG, Buttery, PJ, Wood, JD & Warkup, C (1999) Altered calpain levels in longissimus muscle from normal pigs and heterozygotes with the ryanodine receptor mutation. Journal of Animal Science 77, 2956–2964.CrossRefGoogle ScholarPubMed
Shackelford, SD, Wheeler, TL & Koohmaraie, M (1997a) Repeat- ability of tenderness measurements in beef round muscles. Journal of Animal Science 75, 2411–2416.CrossRefGoogle Scholar
Shackelford, SD, Wheeler, TL & Koohmaraie, M (1997b) Effect of the callipyge phenotype and cooking method on tenderness of several major lamb muscles. Journal of Animal Science 75, 2100–2105.CrossRefGoogle ScholarPubMed
Sinclair, KD, Lobley, GE, Horgan, GW, Kyle, DJ, Porter, AD, Matthews, KR, Warkup, CC & Maltin, CA (2001) Factors influencing beef eating quality 1. Effects of nutritional regimen and genotype on organoleptic properties and instrumental texture. Animal Science 72, 269–277.CrossRefGoogle Scholar
Solomon, MB & West, RL (1985) Profile of fiber types in muscles from wild pigs native to the United States. Meat Science 13, 247–254.CrossRefGoogle ScholarPubMed
Sorimachi, H, Ishiura, S & Suzuki, K (1997) Structure and physiological function of calpains. Biochemistry Journal 328, 721–732.CrossRefGoogle ScholarPubMed
Suzuki, K & Sorimachi, H (1998) A novel aspect of calpain activation. FEBS Letters 433, 1–4.CrossRefGoogle ScholarPubMed
Sylvestre, MN, Balcerzak, D, Feidt, C, Baracos, VE, Brun, Bellut J (2002) Elevated rates of collagen solubilization and post mortem degradation in muscles of lambs with high growth rates: Possible relationship with activity of matrix metalloproteinases. Journal of Animal Science 80, 1871–1878.CrossRefGoogle Scholar
Tarrant, PV (1998) Some recent advances and future priorities for the meat industry. Meat Science 49 Suppl. 1 S1–S16.CrossRefGoogle Scholar
Tatum, JD, Belk, KE, George, MH & Smith, CC (1999) Identification of quality management practices to reduce the incidence of retail beef tenderness problems: Development and evaluation of a prototype quality system to produce tender beef. Journal of Animal Science 77, 2112–2118.CrossRefGoogle ScholarPubMed
Taylor, RG, Geesink, GH, Thompson, VF, Koohmaraie, M & Goll, DE (1995) Is Z-disk degradation responsible for postmortem tenderization?. Journal of Animal Science 73, 1351–1367.CrossRefGoogle ScholarPubMed
Valin, C, Touraille, C, Vigneron, P & Ashmore, CR (1982) Prediction of lamb meat quality traits based on muscle biopsy fibre typing. Meat Science 6, 257–263.CrossRefGoogle ScholarPubMed
Van, Laack, RL, Kauffman RG (1999) Glycolytic potential of red, soft, exudative pork longissimus muscle. Journal of Animal Science 77, 2971–2973.Google Scholar
Van, Laack, RLJM, Stevens, SG, Stalder KJ (2001) The influence of ultimate pH and intramuscular fat content on pork tenderness and tenderisation. Journal of Animal Science 79, 392–397.Google Scholar
Veiseth, E, Shackelford, SD, Wheeler, TL & Koohmaraie, M (2001) Effect of postmortem storage on μ,-calpain and m-calpain in ovine skeletal muscle. Journal of Animal Science 79, 1502–1508.CrossRefGoogle ScholarPubMed
Vestergaard, M, Therkildsen, M, Henckel, P, Jensen, LR, Andersen, HR & Sejrsen, K (2000) Influence of feeding intensity, grazing and finishing feeding on meat and eating quality of young bulls and the relationship between muscle fibre characteristics, fibre fragmentation and meat tenderness. Meat Science 54, 187–195.CrossRefGoogle ScholarPubMed
Wanatabe, A, Daly, CC & Devine, CE (1996) The effects of the ultimate pH of meat on tenderness changes during ageing. Meat Science 42, 67–78.CrossRefGoogle Scholar
Wegner, J, Albrecht, E, Fiedler, I, Teuscher, F, Papstein, H-J & Ender, K (2000) Growth- and breed-related changes of muscle fiber characteristics in cattle. Journal of Animal Science 78, 1485–1496.CrossRefGoogle ScholarPubMed
Wheeler, TL, Shackelford, SD, Casas, E, Cundiff, LV & Koohmaraie, M (2001) The effects of Piedmontese inheritance and myostatin genotype on the palatability of longissimus thoracis, gluteus medius semimembranosus and biceps femoris. Journal of Animal Science 79, 3069–3074.CrossRefGoogle ScholarPubMed
Wheeler, TL, Shackelford, SD & Koohmaraie, M (2000) Variation in proteolysis, sarcomere length, collagen content, and tenderness among major pork muscles. Journal of Animal Science 78, 958–965.CrossRefGoogle ScholarPubMed
Wiegand, BR, Parrish, FC, Jr, Morrical, DG, Huff-Lonergan E (2001) Feeding high levels of vitamin D 3 does not improve tenderness of callipyge lamb loin chops. Journal of Animal Science 79, 2086–2091.CrossRefGoogle Scholar
Wulf, DM, Emnett, RS, Leheska, JM & Moeller, SJ (2002) Relationships among glycolytic potential, dark cutting (dark, firm, and dry) beef, and cooked beef palatability. Journal of Animal Science 80, 1895–1903.CrossRefGoogle ScholarPubMed
Zamora, F, Debiton, E, Lepetit, J, Dransfield, E & Ouali, A (1996) Predicting variability of ageing and toughness in beef m longissimus lumborum et thoracis. Meat Science 43, 321–333.CrossRefGoogle ScholarPubMed