Hostname: page-component-cd9895bd7-p9bg8 Total loading time: 0 Render date: 2024-12-24T14:02:42.943Z Has data issue: false hasContentIssue false
  • English
  • Français

Effect of growth rate on tenderness development and final tenderness of meat from Friesian calves

Published online by Cambridge University Press:  18 August 2016

M. Therkildsen ,
L. Melchior Larsen ,
H. G. Bang  and
M. Vestergaard
M. Therkildsen*
Affiliation:
Danish Institute of Agricultural Sciences, DK-8830 Tjele, Denmark
L. Melchior Larsen
Affiliation:
Royal Veterinary and Agricultural University, DK-1871 Frederiksberg C, Denmark
H. G. Bang
Affiliation:
Danish Meat Research Institute, DK-4000 Roskilde, Denmark
M. Vestergaard
Affiliation:
Danish Institute of Agricultural Sciences, DK-8830 Tjele, Denmark
*
† E-mail: [email protected]
Get access

Abstract

The present study was conducted to determine the effect of growth rate of calves on the activity of the calpain system post mortem, post mortem desmin degradation, myofibrillar fragmentation index and meat tenderness of m. longissimus lumborum (LL) and m. supraspinatus (SS). Twenty-four Friesian heifer calves were allocated to two treatment groups: MM and HH. The MM calves were given food to achieve a moderate growth rate (678 g/day from 5 days of age to 90 kg body weight (BW) (period I) and 770 g/day from 90 kg BW to slaughter at 250 kg BW (period II)) and the HH calves were given food to achieve a high growth rate (period I: 895 g/day and period II: 1204 g/day). The myofibril fragmentation index (MFI), desmin degradation and the activity of µ-calpain, m-calpain and calpastatin were measured in LL and SS at slaughter, and 1 and 7 days post mortem. Shear force was measured in LL and SS after 1 and 7 days of ageing and a sensory panel evaluated the eating quality of the loin aged 7 days. MFI (P < 0·01) and tenderness (P < 0·01) were higher and shear force was lower (P < 0·001) in meat from HH calves compared with meat from MM calves. However, growth rate did not affect the activity of µ-calpain, m-calpain or calpastatin or the degradation pattern of desmin at any time post mortem. Besides growth rate and MFI at day 7 post mortem, which both correlated positively with meat tenderness (P < 0·001 and P < 0·01, respectively), fibre type traits and DNA or RNA concentrations were not generally related to final tenderness. Thus, it was concluded that increased growth rate of calves before slaughter increased the ease of fragmentation (MFI) of the meat and improved the tenderness but these findings could not be related to any changes in the activity of the calpain system.

Keywords

calpaincalvesdesmingrowth ratemyofibrilstenderness
Type
Growth, development and meat science
Information
Animal Science , Volume 74 , Issue 2 , April 2002 , pp. 253 - 264
Copyright
Copyright © British Society of Animal Science 2002

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Aberle, E. D., Reeves, E. S., Judge, M. D., Hunsley, R. E. and Perry, T. W. 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, P. G., Harper, G. S. and Hunter, R. A. 1998. Effect of growth path on the tenderness of the semitendinosus muscle of Brahman-cross steers. Meat Science 48: 65–73.CrossRefGoogle ScholarPubMed
Andersen, H. R., Ingvartsen, K. L. and Klastrup, S. 1984. Influence of energy level, weight at slaughter and castration on carcass quality in cattle. Livestock Production Science 11: 571–586.Google Scholar
Boccard, R. L., Naudé, R. T., Cronje, D. E., Smit, M. C., Venter, H. J. and Rossouw, E. J. 1979. The influence of age, sex and breed of cattle on their muscle characteristics. Meat Science 3: 261–280.CrossRefGoogle ScholarPubMed
Buchter, L. and Andersen, H. R. 1975. Slagtevægtens og foderstyrkens indflydelse på vækst, foderudnyttelse samt slagte-og kødkvalitet hos RDM-ungtyre. III. Kødkvalitet. Meddelelser 77, Statens Husdyrbrugsforsøg, København, Denmark.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. Journal of Animal Science 66: 1186–1193.Google Scholar
Calkins, C. R., Dutson, T. R., Smith, G. C., Carpenter, Z. L. and Davis, G. W. 1981. Relationship of fiber type composition to marbling and tenderness of bovine muscle. Journal of Food Science 46: 708–710.Google Scholar
Cover, S., Hostetler, R. L. and Ritchey, S. J. 1962. Tenderness of beef. IV. Relations of shear force and fibre extensibility to juiciness and six components of tenderness. Journal of Food Science 27: 527–536.Google Scholar
Cross, H. R., Schanbacher, B. D. and Crouse, J. D. 1984. Sex, age and breed related changes in bovine testosterone and intramuscular collagen. Meat Science 10: 187–195.Google Scholar
Crouse, J. D., Koohmaraie, M. and Seideman, S. C. 1991. The relationship of muscle fibre size to tenderness of beef. Meat Science 30: 295–302.Google Scholar
Culler, R. D., Parrish, F. C. Jr, Smith, G. C. and Cross, H. R. 1978. Relationship of myofibril fragmentation index to certain chemical, physical and sensory characteristics of bovine longissimus muscle. Journal of Food Science 43: 1177–1180.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 Ca dependent neutral proteinases and their inhibitor in beef muscle. Meat Science 15: 193–202.CrossRefGoogle ScholarPubMed
Eenaeme, C. Van, Clinquart A., Uytterhaegen, L., Hornick, J., Demeyer, D. and Istasse, L. 1994. Post mortem proteases activity in relation to muscle protein turnover in Belgian Blue bulls with different growth rates. Science des Aliments 14: 475–483.Google Scholar
Ertbjerg, P., Larsen, L. M. and Mølle, A. J. 1999a. Effect of prerigor lactic acid treatment on lysosomal enzyme release in bovine muscle. Journal of the Science of Food and Agriculture 79: 95–100.Google Scholar
Ertbjerg, P., Mielche, M. M., Larsen, L. M. and Møller, A. J. 1999b. Relationship between proteolytic changes and tenderness in prerigor lactic acid marinated beef. Journal of the Science of Food and Agriculture 79: 970–978.Google Scholar
Fishell, V. K., Aberle, E. D., Judge, M. D. and Perry, T. W. 1985. Palatability and muscle properties of beef as influenced by preslaughter growth rate. Journal of Animal Science 61: 151–157.Google Scholar
Geesink, G. and Koohmaraie, M. 1999. Technical note: a rapid method for quantification of calpain and calpastatin activities in muscle. Journal of Animal Science 77: 3225–3229.CrossRefGoogle ScholarPubMed
Geesink, G. H., Laack, R. L. J. M. Van Barnier, V. M. H. and Smulders, F. J. M. 1994. Does electrical stimulation affect the speed of ageing response? Sciences des Aliments 14: 409–422.Google Scholar
Gerhardy, H. 1995. Quality of beef from commercial fattening systems in northern Germany. Meat Science 40: 103–120.Google Scholar
Goll, D. E., Kleese, W. C. and Szpacenko, A. 1989. Skeletal muscle proteases and protein turnover. In Animal growth regulation (ed. Campion, D. R. Hausman, G. J. and Martin, R. J.), pp. 141–182. Plenum Publishing, New York.Google Scholar
Gornall, A. G., Bardawill, C. J. and David, M. M. 1949. Determination of serum proteins by means of biuret reaction. Journal of Biological Chemistry 177: 751–766.Google Scholar
Grunert, K. G. 1997. What’s in a steak? A cross-cultural study on the quality perception of beef. Food Quality and Preference 8: 157–174.Google Scholar
Ho, C., Stromer, M. H. and Robson, R. M. 1996. Effect of electrical stimulation on postmortem titin, nebulin, desmin, and troponin-T degradation and ultrastructural changes in bovine longissimus muscle. Journal of Animal Science 74: 1563–1575.CrossRefGoogle ScholarPubMed
Ho, C., Stromer, M. H., Rouse, G. and Robson, R. M. 1997. Effects of electrical stimulation and postmortem storage on changes in titin, nebulin, desmin, troponin-T, and muscle ultrastructure in Bos indicus crossbred cattle. Journal of Animal Science 75: 366–376.CrossRefGoogle ScholarPubMed
Hoving-Bolink, A.H, Hanekamp, W. J. A. and Walstra, P. 1999. Effects of sire breed and husbandry system on carcass, meat and eating quality of Piemontese and Limousin crossbred bulls and heifers. Livestock Production Science 57: 275–278.Google Scholar
Johnson, M. H., Calkins, C. R., Huffman, R. D., Johnson, D. D. and Hargrove, D. D. 1990. Differences in cathepsins B + L and calcium-dependent protease activities among breed type and their relationship to beef tenderness. Journal of Animal Science 68: 2371–2379.Google Scholar
Koohmaraie, M. 1990. Quantification of Ca2+-dependent protease activities by hydrophobic and ion-exchange chromatography. Journal of Animal Science 68: 659–665.Google Scholar
Koohmaraie, M. 1996. Biochemical factors regulating the toughening and tenderization processes of meat. Meat Science 43: 193–201.CrossRefGoogle 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 Science 19: 187–196.CrossRefGoogle ScholarPubMed
Koohmaraie, M., Shackelford, S.D., Wheeler, T. L., Lonergan, S. M. and Doumit, M. E. 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, D. H., Crouse, J. D. and Mersmann, H. J. 1991. Postmortem proteolysis in longissimus muscle from beef, lamb and pork carcasses. Journal of Animal Science 69: 617–624.Google Scholar
Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685.Google Scholar
Maltin, C. A., Sinclair, K. D., Warriss, P. D., Grant, C. M., Porter, A. D., Delday, M. I. and Warkup, C. C. 1998. The effects 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.Google Scholar
Miller, R. K., Cross, H. R., Crouse, J. D. and Tatum, J. D. 1987. The influence of diet and time on feed on carcass traits and quality. Meat Science 19: 303–313.CrossRefGoogle ScholarPubMed
Morgan, J. B., Wheeler, T. L., Koohmaraie, M., Crouse, J. D. and Savell, J. W. 1993. Effect of castration on myofibrillar protein turnover, endogenous proteinase activities, and muscle growth in bovine skeletal muscle. Journal of Animal Science 71: 408–414.CrossRefGoogle ScholarPubMed
Morrison, E. H., Mielche, M. M. and Purslow, P. P. 1998. Immunolocalisation of intermediate filament proteins in porcine meat. Fibre type and muscle-specific variations during conditioning. Meat Science 50: 91–104.Google Scholar
Møller, A. J., Vestergaard, T. and Wismer-Pedersen, J. 1973. Myofibril fragmentation in bovine longissimus dorsi as an index of tenderness. Journal of Food Science 38: 824–825.CrossRefGoogle Scholar
Olson, D. G. and Parrish, F. C. Jr 1977. Relationship of myofibril fragmentation index to measures of beefsteak tenderness. Journal of Food Science 42: 506–509.CrossRefGoogle Scholar
Olsson, U., Hertzman, C. and Tornberg, E. 1994. The influence of low temperature, type of muscle and electrical stimulation on the course of rigor mortis, ageing and tenderness of beef muscles. Meat Science 37: 115–131.Google Scholar
Ouali, A. and Talmant, A. 1990. Calpains and calpastatin distribution in bovine, porcine and ovine skeletal muscles. Meat Science 28: 331–348.Google Scholar
Pringle, T. D., Williams, S.E., Lamb, B. S., Johnson, D. D. and West, R. L. 1997. Carcass characteristics, the calpain proteinase system, and aged tenderness of Angus and Brahman crossbred steers. Journal of Animal Science 75: 2955–2961.CrossRefGoogle ScholarPubMed
Ritchey, S. J. and Hostetler, R. L. 1965. The effect of small temperature changes on two beef muscles as determined by panel scores and shear-force values. Food Technology 8: 93–95.Google Scholar
Statistical Analysis Systems Institute. 1989. SAS/STAT user’s guide, version 6, fourth edition. SAS Institute Inc., Cary, NC.Google Scholar
Statistical Analysis Systems Institute. 1992. SAS technical report P-229, SAS/STAT software: changes and enhancements, release 6. 07. SAS Institute Inc., Cary, NC.Google Scholar
Scheeder, M. and Langholz, H. J. 1996. Texture properties of ten beef muscles to be marketed as steaks. Proceedings of the 42nd ICoMST, Lillehammer, Norway, pp. 276–277.Google Scholar
Seideman, S. C., Koohmaraie, J. D. and Crouse, J. D. 1987. Factors associated with tenderness in young beef. Meat Science 21: 281–291.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. Journal of Animal Science 72: 857–863.Google Scholar
Shackelford, S.D., Koohmaraie, M., Miller, M. F., Crouse, J. D. and Reagan, J. O. 1991. An evaluation of tenderness of the longissimus muscle of Angus by Hereford versus Brahman crossbred heifers. Journal of Animal Science 69: 171–177.Google Scholar
Shackelford, S.D., Wheeler, T. L. and Koohmaraie, M. 1995. Relationship between shear force and trained sensory panel tenderness ratings of 10 major muscles from Bos indicus and Bos taurus cattle. Journal of Animal Science 73: 3333–3340.CrossRefGoogle ScholarPubMed
Steen, D., Claeys, E., Uytterhaegen, L., Smet S, de and Demeyer, D. 1997. Early post-mortem conditions and the calpain/calpastatin system in relation to tenderness of double-muscle beef. Meat Science 45: 307–319.CrossRefGoogle Scholar
Taylor, R. G., Geesink, G. H., Thompson, V. F., Koohmaraie, M. and Goll, D. E. 1995a. Is Z-disk degradation responsible for postmortem tenderization? Journal of Animal Science 73: 1351–1367.Google Scholar
Taylor, R. G., Goll, D. E. and Ouali, A. 1995b. Enzyme localization during postmortem muscle tenderization. In Expression of tissue proteinases and regulation of protein degradation as related to meat quality (ed. Ouali, A. Demeyer, D. I and Smulders, F.J. M.), pp. 347–358. ECCEAMST, Utrecht, The Netherlands.Google Scholar
Taylor, R. G. and Koohmaraie, M. 1998. Effects of post mortem storage on the ultrastructure of the endomysium and myofibrils in normal and callipyge longissimus. Journal of Animal Science 76: 2811–2817.Google Scholar
Therkildsen, M., Melchior Larsen, L. and Vestergaard, M. 2002. Influence of growth rate and muscle type on muscle fibre type characteristics, protein synthesis capacity and activity of the calpain system in Friesian calves. Animal Science 74: 243–251.CrossRefGoogle Scholar
Therkildsen, M., Vestergaard, M., Jensen, L. R., Andersen, H. R. and Sejrsen, K. 1998. Effect of feeding level, grazing and finishing on growth and carcass quality of young Friesian bulls. Acta Agriculturæ Scandinavica, Section A, Animal Science 48: 193–201.Google Scholar
Thomson, B. C., Muir, P. D. and Dobbie, P. M. 1999. Effect of growth path and breed on the calpain system in steers finished in a feedlot. Journal of Agricultural Science, Cambridge 133: 209–215.CrossRefGoogle Scholar
Towbin, H., Staehelin, T. and Gordon, J. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proceedings of the National Academy of Sciences of the United States of America 76: 4350–4354.Google Scholar
Vestergaard, M., Therkildsen, M., Henckel, P., Jensen, L. R., Andersen, H. R. and 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.Google Scholar
Weber, A., Wassilev, K., Møller, A. J., Schmidt-Nielsen, B. and Glad, F. 1988. Computerized laser diffractometer for routine measurements of sarcomere lengths in meat. Journal of Food Science 53: 691–695.Google Scholar
Wheeler, T. L. and Koohmaraie, M. 1992. Effects of the β-adrenergic agonist L644,969 on muscle protein turnover, endogenous proteinases activities, and meat tenderness in steers. Journal of Animal Science 70: 3035–3043.Google Scholar
Wheeler, T. L. and Koohmaraie, M. 1999. The extent of proteolysis is independent of sarcomere length in lamb longissimus and psoas major. Journal of Animal Science 77: 2444–2451.Google Scholar
Wheeler, T. L., Shackelford, S.D. and Koohmaraie, M. 1999. Tenderness classification of beef. III. Effect of the interaction between end point temperature and tenderness on Warner-Bratzler shear force of beef longissimus. Journal of Animal Science 77: 400–407.Google Scholar
Whipple, G. and Koohmaraie, M. 1991. Degradation of myofibrillar proteins by extractable lysosomal enzymes and m-calpain, and the effects of zinc chloride. Journal of Animal Science 69: 4449–4460.CrossRefGoogle ScholarPubMed
Whipple, G. and Koohmaraie, M. 1992. Effects of lamb age, muscle type, and 24-hour activity of endogenous proteinases on postmortem proteolysis. Journal of Animal Science 70: 798–804.Google Scholar
Whipple, G., Koohmaraie, M., Dikeman, M. E. and Crouse, J. D. 1990. Predicting beef-longissimus tenderness from various biochemical and histological muscle traits. Journal of Animal Science 68: 4193–4199.CrossRefGoogle ScholarPubMed