EFFECT OF ROUGHAGE TO CONCENTRATE RATIO ON QUALITATIVE AND QUANTITATIVE CHARACTERISTICS OF VEAL CARCASSES
DOI:
https://doi.org/10.36103/jne46z43Keywords:
longissimus dorsi, biceps femoris, semimembranosus, muscle location, roughage, IMF, marblingAbstract
This study was conducted in the animal farm of the College of Agricultural Engineering Sciences/ University of Baghdad/ Iraq, from 23 march 2014 to 23 may 2014 to investigate the effect of two levels of roughage to concentrate ratio on qualitative and quantitative characteristics of Holstein Friesian veal’s, by studying the traits of three major muscles (longissimus dorsi LD, biceps femoris BF and semimembranosus SM). Two equal groups of Holstein Friesian veal’s were used. Each group was consilted of five veal’s at eight months old and weighted 228.800 ± 21.221Kg and 227.800 ± 9.167 Kg respectively. Lean chemical composition were studied with characteristics (pH, WHC, TVN, TBA, P.V, FFAs, myoglobin concentrations Mb and protein solubility PS). The results were confirming that a high effect of the diets contents on the muscles properties especially the fat contents. The muscle location had a strong effect too on muscle properties. LD muscle was in high difference always with the other two, in spite of the differences among all kinds of muscle in all traits.
Received: 12/3/2025
Accepted: 16/6/2025
Published: 2026/4/30
References
A.O.A.C. 1980. Official Methods of Analysis, 13th ed. Association of Official Analytical Chemists. Washington, DC.
Aberle, E. D., J. C. Forrest, D. E. Gerrard, E. W. Mills, H. B. Hedrick, M. D. Judge & R. A. Merkel. 2001. Principles of Meat Science (4th edition), Kendall/Hunt Publishing Company, 4050 Westmark Drive, Dubuque, Iowa, USA. p. 94.
Alina H. & T. Ovidiu. 2007. Determination of total protein in some meat products. Analele Stuntificeale University, Alexandru Ioan Cuza, Sectiunea Genetica si Biologie Moleculara, TOM VIII.
Asp, M.L., J. R. Richardson, A.L. Collene, K.R. Droll, & M.A. Belury. 2012. Dietary protein and beef consumption predict for markers of muscle mass and nutrition status in older adults. J. Nutr. Health Aging, 16, 784–790.
Barendse, W., R.J. Bunch, M.B. Thomas, & B.E. Harrison. 2009. A splice site single nucleotide polymorphism of the fatty acid binding protein 4 gene appears to be associated with intramuscular fat deposition in longissimus muscle in Australian cattle. Anim. Genet., 40, 770–773.
Butterfield, R.M., J. Zamora, J.M. Thompson & J. Williams. 1983. Changes in body composition relative to weight and maturity in large and small strains of Australian Merino rams. ll. Individual muscle groups. Anim. Prod. 36,165-174.
Cole, N. A., R. R. Johnson, F. N. Owens, & J. R. Males. 1976. Influence of roughage level and corn processing method on microbial protein synthesis by beef steers. J. Anim. Sci. 43:497-503
Dave, D. & A.E. Ghaly. 2011. Meat spoilage mechanisms and preservation techniques: A critical review. American Journal of Agricultural and Biological Sciences 6 (4): 486-510.
Denhertog-Meischke, M.J.A., F.J.M. Smulderes, Vanloglestijn, and F. Vanknapen. 1997. The effects of electrical stimulation on the water holding capacity and protein denaturation of two bovine muscle. J. Anim. Sci. 75:118-124.
Dolatowski, J. Z. & D. M. Stasiak. 1998. The effect of low frequency and intensity ultrasound on pre-rigor meat on structure and functional parameters of freezing and thawed beef semimemb-ranosus muscle. Proc. 44th Int. Cong. Meat. Sci. Technol., Barcelona, Spain.
Egan, H., R. S. Kirk, & R. Sawyer. 1981. Pearon’s chemical Analysis of Food. Bulter and Tanner Ltd. Brtain.
Ertbjerg, P., and E. Puolanne. 2017. Muscle structure, sarcomere length and influences on meat quality: A review. Meat Sci. 132:139-152.
Felista W.M., E. Charmley, P.G. Christopher, S. M. Bunmi, T. K. Robert, & E. O. Aduli. 2019. Diet and genetics influence beef cattle performance and meat quality characteristics. Foods. Vol.8 (Issue 12) 648.
Gheisari, H. R. 2011. Correlation between acid, TBA, peroxide and iodine values, catalase and glutathione peroxidase activities of chicken, cattle and camel meat during refrigerated storage. Veterinary World, Vol.4(4):153-157.
Guttmann, R. P., & G. V. Johnson. 1998. Oxidative stress inhibits calpain activity in situ. Journal of Biological Chemistry, 273, 13331–13338.
Hassanin, F. S., M. A. Hassan, F. A. Shaltouta, N.A. Shawqyb, & G. A. Abd-Elhameed. 2017. Chemical criteria of chicken meat. Benha Veterinary Medical Journal, V.33, No (2):457-464.
Hocquette, J.F., F. Gondret, E. Bae´za, F. Me´dale, C. Jurie, & D. W. Pethick. 2009. Intramuscular fat content in meat-producing animals: development, genetic and nutritional control, and identification of putative markers. Animal (2010), 4:2, pp 303–319 and the Animal Consortium. doi:10.1017/S1751731109991091.
Hocquette, J.F., I. Ortigues-Marty, D.W. Pethick, P. Herpin, and X. Fernandez. 1998. Nutritional and hormonal regulation of energy metabolism in skeletal muscles of meat-producing animals. Livestock Production Science 56, 115–143.
Hocquette, J.F., P. Bas, D. Bauchart, M. Vermorel, & Y. Geay. 1999. Fat partitioning and biochemical characteristics of fatty tissues in relation to plasma metabolites and hormones in normal and double-muscled young growing bulls. Comparative Biochemistry and Physiology Part A: Physiology 122,127–138.
Hodgson, R.R., G.W. Davis, G.C. Smith, J.W. Savelli, & H.R. Cross. 1991. Relationships between pork loin palatability traits and physical characteristics of cooked chops. Journal of Animal Science 6912, 4858–4865.
Huff-Lonergan, E. & S. Lonergan. 1999. Postmortem mechanisms of meat tenderization: the roles of the structural proteins and the calpain system. In Y. L. Xiong, C.-T. Ho, & F. Shahidi (Eds.), Quality attributes of muscle foods (pp. 229–251). New York: Kluwer Academic/Plenum Publishers.
Huff-Lonergan, E. & S. Lonergan. 2005. Mechanisms of water-holding capacity of meat: The role of postmortem biochemical and structural changes Meat Science 71; 194–204.
Immonen, K., M. Ruusunen, K. Hissa, & E. Puolanne. 2000. Bovine muscle glycogen concentration in relation to finishing diet, slaughter and ultimate pH. Meat Sci., 55, 25–31.
Jihad, M.Q., A.S. Mazahreh, & A.F. Al-Shawabkeh. 2009. Nutritive value of seven varieties of meat products (Sausage) produced in Jordan. Pakistan Journal of Nutrition, 8: 332-334.
Josephson, R. 1993. Contraction dynamics and power output of skeletal muscle. Annu. Rev. Physiol., 55, 527–546.
Juncher, D., B. Ronn, E.T. Mortensen, P. Henckel, A. Karlsson, & L.H. Skibsted. 2001. Effect of pre-slaughter physiological conditions on the oxidative stability of colour and lipid during chill storage of pork. Meat Science, 58, 347–357.
Lefaucheur, L.A. 2010. Second look into fiber typing—Relation to meat quality. Meat Sci., 84, 257–270.
Luna, R., M. A. Hashem, M. S. Ali, M.M. Hossain, M.A. Talukde, & M.S. Islam. 2012. Effect of salt and storage temperature on beef sausage quality. Progress. Agric. 23(1 and 2): 15 – 24, 2012.
Lund, M. N., M. Heinonen, C. P. Baron, and M. Estévez. 2011. Protein oxidation in muscle foods: A review. Mol. Nutr. Food Res. 55:83-95.
Mahmood, M. R. 2015. Determining the quality of chilled and frozen beef Meat in different regions of Iraq Using Biogenic Amines analysis and PCR technique. A thesis / College of Agriculture / University of Baghdad.
Melody, J. L., S. M. Lonergan, L. J. Rowe, T. W. Huiatt, M. S. Mayes, & E. Huff-Lonergan. 2004. Early postmortem biochemical factors influence tenderness and water-holding capacity of three porcine muscles. Journal of Animal Science, 82, 1195–1205.
Michal, J.J., Z.W. Zhang, C.T. Gaskins, & Z. Jiang. 2006. The bovine fatty acid binding protein 4 gene is significantly associated with marbling and subcutaneous fat depth in Wagyu x Limousin F2 crosses. Anim. Genet., 37, 400–402.
Muir, P., J. Deaker, & M. Bown. 1998. Effects of forage-and grain-based feeding systems on beef quality: A review. New Zealand J. Agric. Res., 41, 623–635.
Newcom, D.W., T.J. Baas, & J.F. Lampe. 2002. Prediction of intramuscular fat percentage in live swine using real-time ultrasound. Journal of Animal Science 80, 3046–3052.
OECD. 2019. Meat Consumption. OECD-FAO agricultural Outlook 2018-2027. Available online: https://www.oecd-ilibray.org/agricultureand-food/oecd-fao-agricultur-outlook-2018-2927_agr_outlook-2018-en .
Offer, G. 1991. Modeling of the formation of pale, soft and exudative meat – effects of chilling regime and rate and extent of glycolysis. Meat Science, 30, 157–184.
Park, S.J., S.H. Beak, D.J.S. Jung, S.Y. Kim, I.H. Jeong, M.Y. Piao, H.J. Kang, D.M. Fassah, S.W. Na, & S.P. Yoo. 2018. Genetic, management and nutritional factors affecting intramuscular fat deposition in beef cattle—A review. Asian Australas. J. Anim. Sci., 31, 1043–1061.
Pearson, A. M. & T.R. Dustson. 1985. Advance in Meat Research. Avi Publishing Company, INC. Westport, Connecticut.
Pette, D. and R.S. Staron. 2000. Myosin isoforms, muscle fiber types, and transitions. Microsc. Res. Tech., 50, 500–509.
Picard, B., J. Robelin, & Y. Geay. 1995. Influence of castration and postnatal energy restriction on the contractile and metabolic characteristics of bovine muscle. In Annales de Zootechnie, 44, 347–357.
Rhoades, R.D., J.E. Sawyer, K.Y. Chung, M.L. Schell, D.K. Lunt, & S.B. Smith. 2007. Effect of dietary energy source on in vitro substrate utilization and insulin sensitivity of muscle and adipose tissues of Angus and Wagyu steers. Journal Animal Science 85, 1719–1726.
Rodríguez, R., S. Areadne, & R. Yeni. 2007. Microbial protein synthesis in rumen and its importance to ruminants. Cuban Journal of Agricultural Science, Vol 41, No (4): 287.
SAS. 2001. SAS Statistics (Version 6.0) SAS Inst. Inc.Cary.NC. USA.
Valsta, L.M., H. Tapanainen, & S. Mannisto. 2005. Meat fats in nutrition. Meat Science 70, 525–530.
Verma, A.K., V. Lakshmanan, A.K. Da, S. K. Mendiratta, & A.S.R. Anjaneyulu. 2005. Amer. J. Food Tech. 3: 134 – 140.
Vestergaard, M., N. Oksbjerg, & P. Henckel. 2000. Influence of feeding intensity, grazing and finishing feeding on muscle fibre characteristics and meat colour of semitendinosus, longissimus dorsi and supraspinatus muscles of young bulls. Meat Sci., 54, 177–185.
Weiss, A., S. Schiaffino, & L.A. Leinwand. 1999. Comparative sequence analysis of the complete human sarcomeric myosin heavy chain family: Implications for functional diversity. J. Mol. Biol., 290, 61–75.
WHO. 2003. Diet, nutrition and the prevention of chronic diseases. Report of a joint WHO/FAO expert consultation. WHO technical report series 916, Geneva.
Wicks, J., M. Beline, J. F. Gomez, S. Luzardo, S. Silva, & D. Gerrard. 2019. Muscle Energy Metabolism, Growth, and Meat Quality in Beef Cattle. Agriculture, 9,195; doi:10.3390/agriculture9090195 www.mdpi.com/journal/agriculture
Williams, P. 2007. Nutritional composition of red meat. J. Nutr. Diet., 64, S113–S119.
Williams, P., V. Droulez, & G. Levy. 2006. Nutrient composition of Australian red meat. Gross composition data. Food Aust; 58(1): 173-181.
Williams, P., V. Droulez, & G. Levy. 2002. Composition of Australian red meat. Nutrient profile. Food Aust; 59 (3).
Witte, V. C., G. Krause, & M. E. Bailey. 1970. New extraction method for deter mining 2-thiobarbituric acid values of pork and beef during storage. J. Food Sci., 35:582-585.
Wittenberg, B., J. Wittenberg, & P. Caldwell. 1975. Role of myoglobin in the oxygen supply to red skeletal muscle. J. Biol. Chem., 250, 9038–9043.
Wittenberg, J.B. 1970. Myoglobin-facilitated oxygen diffusion: Role of myoglobin in oxygen entry into muscle. Physiol. Rev., 50, 559–636.
Wolcott, M.L., D.J. Johnston, S.A. Barwick, C.L. Iker, J.M. Thompson, & H.M. Burrow. 2009. Genetics of meat quality and carcass traits and the impact of tender stretching in two tropical beef genotypes. Anim. Prod. Sci., 49, 383–398.
Zessin, D.A., C.V. Pohu, G.D. Wilson, & D.S. Carrigan. 1961. Effect of pre-slaughter dietary stress on the carcass characteristics and palatability of pork. J. Anim. Sci. 20: 871-876.
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