Asian Journal of Dairy and Food Research, volume 40 issue 4 (december 2021) : 371-375

​Biochemical and Physicochemical Characteristics in Different Skeletal Muscles of Sheep Hind Limb

Gangadhar Kapase1, Shrikant Kulkarni1, Kiran Mohan2,*, Gurubasayya Panchaxarayya Kalmath3, Kartikesh Sidramayya Math1
1Department of Veterinary Physiology and Biochemistry, Veterinary College, Bidar, Karnataka Veterinary, Animal and Fisheries Sciences University, Nandinagar-585 401, Karnataka, India.
2Department of Livestock Products Technology, Veterinary College, Bidar, Karnataka Veterinary, Animal and Fisheries Sciences University, Nandinagar-585 401, Karnataka, India.
3Department of Veterinary Physiology and Biochemistry, Veterinary College Hebbal, Karnataka Veterinary, Animal and Fisheries Sciences University, Bengaluru-560 024, Karnataka, India.
Cite article:- Kapase Gangadhar, Kulkarni Shrikant, Mohan Kiran, Kalmath Panchaxarayya Gurubasayya, Math Sidramayya Kartikesh (2021). ​Biochemical and Physicochemical Characteristics in Different Skeletal Muscles of Sheep Hind Limb . Asian Journal of Dairy and Food Research. 40(4): 371-375. doi: 10.18805/ajdfr.DR-1608.
Background: High variation in meat quality has been reported between animals and within muscles of same animals. An understanding of these variations is a pivotal step to design strategies for better utilization of such meat while producing high quality meat to consumers. The current study was aimed to unravel biochemical and physico-chemical profile of sheep hind limb.

Methods: The sheep hind limb was procured from traditionally slaughtered sheep immediately after exsanguination. The Vastus lateralis (VL), Gluteo biceps femoris (GBF), Gluteomedius (GM), Longissimus thoracis et lumborum (LTL), Psoas major (PM) and Semitendinosus (ST) muscles were separated from hot boned carcass of sheep. Each hot boned muscle was cut and analysed for biochemical and physico-chemical characteristics.

Result: There was significant (p<0.05) variation in water holding capacity, protein extractability (Sarcoplasmic, myofibrillar and total), collagen content, collagen solubility and instrumental colour value among different skeletal muscles studied. Non-significant (p>0.05) variations were found in parameters like pH, drip loss, myofibrillar fragmentation index, muscle fibre diameter and Warner Bratzler shear force values. The Gluteo biceps femoris muscle was found to have higher myoglobin; myofibrillar fragmentation index and Warner Bratzler shear force values with lowest protein extractability values. The collagen content in the Gluteo biceps femoris was significantly (p<0.05) higher with lowest collagen solubility (15.32%) as compared to other muscles.
Livestock is a natural resource with rural people of India. Almost 70 per cent of people living in villages are poor and depend on agriculture and livestock activities for their livelihood, income and employment. In the livestock sector, sheep and goats are  reared by a very large number of poor, socially backward and economically weaker sections of rural people for whom these animals are important since they provide employment and income from milk, meat, wool, skin and manure and are often a ready source of ‘cash-income’ during the periods of drought and scarcity. India has 74.26 million Sheep accounting for 13.8% of the total livestock population in India (DAHF, 2019).
       
Carcass and meat compositions are dependent on rearing practices, breed, gender, weight and the management of the animals before slaughter. The skeletal muscle is mainly composed of different types of muscle fibers varying in their molecular, metabolic, structural and contractile properties (Choi and Kim, 2009). The quality of meat is dependent on palatability, wholesomeness and safety. The palatability of meat is influenced by tenderness, flavour and juiciness. The characterization of meat quality of different skeletal muscles has been well documented in beef and pork (Jones et al., 2001; Jones and Burson, 2000). High inter species and intra species variations are seen among muscle fibers due to adaptations to different activities by a muscle (Hopkins and Fogarty, 1998). Genetic and environmental factors influence the technological and organoleptic attributes of meat by affecting muscle structure and muscle biochemistry (Hopkins and Fogarty, 1998). In numerous studies, the quality characteristics of sheep meat have been reported (Gardener et al., 1999; Warriss et al., 1990).
       
However, the comprehensive reports on variation in biochemical and physico-chemical characteristics in different skeletal muscles of sheep are relatively scarce. Such information on individual characteristics of muscle is vital, as it can benefit the processor by improving meat quality along with providing a hint on processing technologies to be adopted based on individual characteristics of muscle. The aim of this study was to unravel variation in biochemical and physico-chemical characteristics of different skeletal muscles of sheep.
The sheep hind limb was procured from traditionally slaughtered sheep immediately after exsanguination at local slaughterhouse of Bidar, Karnataka. The Vastus lateralis (VL), Gluteo biceps femoris (GBF), Gluteomedius (GM), Longissimus thoracis et lumborum (LTL), Psoas major (PM) and Semitendinosus (ST) muscles were separated from hot boned carcass of sheep. Each muscle was cut, packed in low density polyethylene bags and stored under refrigerated conditions (4±1°C) in domestic refrigerator and were analyzed for biochemical and physico-chemical characteristics.
 
Biochemical and physicochemical analysis
 
The pH of muscle sample was measured using a digital pH meter (Naveena et al., 2004). For determining water-holding capacity, centrifugal method of estimation was used (Wardlaw et al., 1973). Drip loss was determined according to the procedure of Honikel and Hamm (1994). Protein extractability was determined using procedure as outlined by Joo et al., (1999). Collagen content (Dransfield et al., 1983) and collagen solubility (Mahendrakar et al., 1989) was determined through estimation of Hydroxyproline based on the procedure of Nueman and Logan (1950). Myofibrillar fragmentation index was calculated as per the procedure outlined by Davis et al., (1980). The MFI was reported as the weight of the residue in gram percentage. Muscle fibre diameter was determined as described by Tuma et al., (1962) using calibrated micrometer. The Warner-Bratzler shear force (WBSF) of the cores were measured using Texturometer (Model: Shimazdu EZ-SX Table top texture analyser, Japan) with V-shaped stainless-steel blade (60° angle). Myoglobin was extracted from muscle using a modified procedure of Warris (1979) and concentration was calculated according to Trout (1989). Colour values (CIE b*) of the muscle samples were determined using a hand-held colorimeter (Model: CR10 Plus Konica Minolta limited Inc, Japan).
 
Statistical analysis
 
Statistical analysis of results was performed by ANOVA using SPSS (SPSS version 13.0 for windows; SPSS, Chicago, IL, USA). Least square means for F-tests were calculated using Duncan’s multiple range tests and were considered significant at p<0.05.
Results of changes in biochemical and physico-chemical properties between various skeletal muscles of hind limb of sheep meat is tabulated in Table 1.
 

Table 1: Biochemical and physico-chemical properties of hot boned raw sheep meat.


 
pH, water holding capacity (WHC) and drip loss
 
In present study, there was no significant (p>0.05) difference in pH of different skeletal muscles. Mean pH values obtained from muscles was within the desired range for quality meat. The approximate postmortem muscle pH depending on species ranges from 5.6 to 5.8. Any alteration in pH drop can influence meat quality (English et al., 2016). The pH values higher than 6.0 are related to lower meat quality (Pratiwi et al., 2007). The WHC of different skeletal muscles studied in this experiment ranged from 23.11% in ST and GM to 26.67% in LTL were significantly (p<0.05) different. WHC values ranged from 22 to 24% among the kids of different breeds and SM muscle had higher water holding capacity than LTL (Das and Rajkumar,2010). Drip loss is a measurement of fresh meats ability to hold water throughout aging. A non significant (p>0.05) difference in the drip loss was observed between different muscles contradicting with WHC values indicating presence of variation in free water in fresh muscles.
 
Protein extractability
 
The highest TPE, SPE and MFPE were found in GM (362.78 mg/g), LTL (151.28 mg/g) and ST (222.38 mg/g) respectively where as the lowest extractability was found in GBF muscle. Muscle protein extractability is affected by pH, salt concentration, type of salts and temperature (Denise, 2001). Lan et al., (1993) concluded that besides pH and muscle fiber type, the extraction condition has a large influence on amount and composition of proteins extracted from muscles. Hence, the muscle specific variations in the protein extractability may be attributed for difference in abundance of different types of muscle fibers in different muscles (Close, 1972).
 
Collagen content and collagen solubility
 
The collagen content of GBF was significantly (p<0.05) higher as compared to other muscles. The collagen content of the skeletal muscles in the current study is in agreement with other studies in sheep (Hopkins et al., 2013; Allingham et al., 2009). The lowest collagen solubility was observed in VL (21.77%) and highest was observed in LTL (31.14%).  Collagen solubility was found in increasing order in VL (21.77%), GBF (26.00%), GM (26.75%), PM (28.40%), ST (30.72%) and LTL (31.14%) muscles. Collagen content also varies significantly between different muscles in pigs (Wheeler et al., 2000). Greater abundance of collagen is found in muscles that are more active physically compared to muscles that are less active, such as the Psoas major (Nishimura et al., 2009).
 
Myofibrillar fragmentation index (MFI) and muscle fibre diameter
 
MFI values of different skeletal muscles did not differ significantly (p>0.05) among different muscles under study. The similar MFI values are reported in buffalo (Naveena et al., 2011) and sheep (Sen et al., 2004; Veiseth et al., 2001) meat. There was no significant (p>0.05) difference in the muscle fiber diameter between different muscles. The highest muscle fiber diameter was observed in ST among the skeletal muscles studied in this experiment.
 
Warner-Bratzler shear force (WBSF), myoglobin (Mb) and colour index (b*)
 
Meat tenderness is affected by the structure of the connective tissue, carcass fatness and collagen levels of meat (Diaz et al., 2002). The WBSF values indicated no significant (p>0.05) difference in the shear force values between different skeletal muscles contrast to findings of Rhee et al., (2004) in beef. Sullivan and Calkins (2011) reported that muscle with WBSF value less than 4.5 kg (44.1 N) had good sensory scoring. All the muscles studied under present experiment were found to be in intermediate to tough tenderness with WBSF ranging 36.28-39.07 N (Boleman et al., 1997).
       
A Significant (p<0.05) difference in the Mb content of VL (3.78 mg/g), GBF (4.33 mg/g), GM (4.01 mg/g), LTL (3.71 mg/g), PM (3.66 mg/g) and ST (2.80 mg/g) muscles were observed in this study. The Mb content of meat varies from 2.7 to 9.4 mg/g depending upon the type of muscle and age (Valin et al., 1984). There was significant (p<0.05) difference in variability of color indices indicating rate and extent of protein denaturation is different among different skeletal muscles under study. The b* was significantly (p<0.05) higher in ST (9.72) and PM (9.64) as compared to VL (8.86), GBF (9.39), GM (8.75) and LTL (8.28). Change in color characteristics of goat meat are highly influenced by postmortem pH (Simela et al., 2004). Yellowness in meat is not generally appreciated by consumers worldwide (Priolo et al., 2002).
The results of current study indicated complex nature of meat quality development with variation in biochemical and physicochemical parameters between different muscles. Exploring the variation in meat quality between muscles is a pivotal step to design strategies for better utilization of such meat while producing highly palatable product to consumers. The results of current study unravel the sources of variation in meat quality among different muscles and provide a basis for the muscle-specific strategies to be adopted for improved quality and value of muscles.

  1. Allingham, P.G., Barris, W., Reverter, A., Hilsenstein, V., van de Ven, R. and Hopkins, D.L. (2009). Sire and growth path effects on sheep meat production 3. Fascicular structure of lamb loin muscle (M. Longissimus lumborum) and the impact on eating quality. Animal Production Science. 49(3): 239-47.

  2. Boleman, S.J., Boleman, S.L., Miller, R.K., Taylor, J.F., Cross, H.R., Wheeler, T.L., Koohmaraie, M., Shackelford, S.D., Miller, M.F., West, R.L. and Johnson, D.D. (1997). Consumer evaluation of beef of known categories of tenderness. Journal of Animal Science. 75(6): 1521-24. 

  3. Choi, Y. M. and Kim, B.C. (2009). Muscle fiber characteristics, myofibrillar protein isoforms and meat quality. Livestock Science. 122(2-3): 105-118.

  4. Close, R.I. (1972). Dynamic Mammalian Properties of Skeletal Muscles. Physiological Reviews. 52: 129- 97.

  5. Das, A.K. and Rajkumar, V. (2010). Comparative study on carcass characteristics and meat quality of three Indian goat breeds. Indian Journal of Animal Sciences. 80(10):1014.

  6. Davis, G.W., Dutson, T.R., Smith, G.C. and Carpenter, Z.L. (1980). Fragmentation of bovine longissimus muscle as an index of cooked steak tenderness. Journal Food Science. 45: 880.

  7. Denise, M.S. (2001). Functional Properties of Muscle Proteins in Processed Poultry Products. In: Poultry Meat Processing, [(Eds) Alan, R Sams]. CRC Press.181-94.

  8. Department of Animal Husbandry and Diarying (2019). 20th Livestock Census. All India Report, Ministry of Fisheries, Animal Husbandry and Dairying, Animal Husbandry Statistics Division. Krishi Bhawan, New Delhi.

  9. Diaz, M.T., Velasco, S., Caneque, V., Lauzurica, S., De Huidobro, F.R., Perez, C., Gonzalez, J. and Manzanares, C. (2002). Use of concentrate or pasture for fattening lambs and its effect on carcass and meat quality. Small Ruminant Research. 43(3): 257-68.

  10. Dransfield, E., Casey, J.C., Boccard, R., Touraille, C., Buchter, L., Hood, D.E., Joseph, R.L., Schon, I., Casteels, M., Casentino, E. and Thimbergen, B.J. (1983). Comparison of chemical composition of meat determined at eight laboratories. Meat Science. 8(2): 79-92.

  11. English, A.R., Wills, K.M., Harsh, B.N., Mafi, G.G., VanOverbeke, D.L. and Ramanathan, R. (2016). Effects of aging on the fundamental color chemistry of dark-cutting beef. Journal of Animal Science. 94(9): 4040-48.

  12. Gardener, G.E., Kennedy, L., Milton, J.T.B. and Pethick, D.W. (1999). Glycogen metabolism and ultimate pH of muscle in Merino, first-cross and second-cross whether lambs as affected by stress before slaughter. Australian Journal of Agricultural Research. 50: 175-81.

  13. Honikel, K.O. and Hamm, R. (1994). Measurement of Water-holding Capacity and Juiciness. In: Quality Attributes and Their Measurement in Meat, Poultry and Fish Products. 24: 125-61. 

  14. Hopkins, D.L. and Fogarty, N.M. (1998). Diverse lamb genotypes-2. Meat pH, colour and tenderness. Meat Science. 49(4): 477-88.

  15. Hopkins, D.L., Allingham, P.G., Colgrave, M. and Van de Ven, R.J. (2013). Interrelationship between measures of collagen, compression, shear force and tenderness. Meat Science 95(2): 219-23.

  16. Jones, S.J. and Burson, D.E. (2000). Porcine myology. Available from http://porcine.unl.edu.

  17. Jones, S.J., Burson, D.E. and Calkins, C.R. (2001). Muscle proûling and bovine myology. Available from http://bovine.unl.edu

  18. Joo, S.T., Kauffman, R.G., Kim, B.C. and Park, G.B. (1999). The relationship of sarcoplasmic and myofibrillar protein solubility to colour and water holding capacity in porcine longissimus muscle. Meat science 35: 276-78.

  19. Lan, Y.H., Novakofski, J., Carr, T.R. and McKeith, F.K. (1993). Assay and storage conditions affect yield of salt soluble protein from muscle. Journal of Food Science. 58(5): 963-67.

  20. Mahendrakar, N.S., Dani, N.P., Ramesh, B.S. and Amla, B.L. (1989). Studies on influence of age of sheep and post mortem carcass conditioning treatments on muscular collagen content and its thermo liability. Journal of Food Science and Technology. 26: 102-05.



  21. Neuman, R.E. and Logan, M.A. (1950). The determination of hydroxyproline. Journal of Biological Chemistry. 184: 299- 06.

  22. Nishimura, T., Fang, S., Wakamatsu, J.I. and Takahashi, K. (2009). Relationships between physical and structural properties of intramuscular connective tissue and toughness of raw pork. Journal of Animal Science. 80: 85-90.

  23. Pratiwi, N.W., Murray, P.J. and Taylor, D.G. 2007. Feral goats in Australia: A study on the quality and nutritive value of their meat. Meat Science. 75(1): 168-77.

  24. Priolo, A., Micol, D., Agabriel, J., Prache, S. and Dransfield, E. (2002). Effect of grass or concentrate feeding systems on lamb carcass and meat quality. Meat Science. 62(2): 179-85.

  25. Rhee, M.S., Wheeler, T.L., Shackelford, S.D. and Koohmaraie, M. (2004). Variation in palatability and biochemical traits within and among eleven beef muscles. Journal of Animal Science. 82: 534-50.

  26. Sen, A.R., Santra, A. and Karim, S.A. (2004). Carcass yield, composition and meat quality attributes of sheep and goat under semiarid conditions. Meat Science. 66: 757- 63.

  27. Simela, L., Webb, E.C. and Frylinck, L. (2004). Effect of sex, age and pre-slaughter conditioning on pH, temperature, tenderness and colour of indigenous South African goats. South African Journal of Animal Science. 34: 1-8.

  28. Sullivan, G.A. and Calkins, C.R. (2011). Ranking beef muscles for Warner–Bratzler shear force and trained sensory panel ratings from published literature. Journal of Food Quality. 34: 195-03.  

  29. Trout, G.R. (1989). Variation in myoglobin denaturation and color of cooked beef, pork and turkey meat as influenced by pH, sodium chloride, sodium tripolyphosphate and cooking temperature. Journal of Food Science. 54(3): 536-40.

  30. Tuma, H.J., Venable, J.H., Wuthier, P.R. and Henrickson, R.L. (1962). Relationship of fibre diameter to tenderness and meatiness as influenced by bovine age. Journal of Animal Science. 21: 33-36.

  31. Valin, C., Pinkas, A., Dragnev, H., Boikovski, S. and Polikronov, D. (1984). Comparative study of buffalo meat and beef. Meat Science. 10(1): 69-84.

  32. Veiseth, E., Shackelford, S. D., Wheeler, T.L. and Koohmaraie, M. (2001). Comparison of myofibril fragmentation index from fresh and frozen pork and lamb longissimus. Journal of Animal Science. 79(4): 904-06.

  33. Wardlaw, F.B., Maccaskill, L.H. and Acton, J.C. (1973). Effect of postmortem muscle changes in poultry meat loaf properties. Journal of Food Science 38: 421-24.

  34. Warris, P.D. (1979). The extraction of haem pigments from fresh meat. International Journal of Food Science and Technology. 14(1): 75-80.

  35. Warriss, P.D., Kestin, S.C., Young, C.S., Bevis, E.A. and Brown, S.N. (1990). Effect of preslaughter transport on carcass yield and indices of meat quality in sheep. Journal of the Science of Food and Agriculture. 51(4): 517-23.

  36. Wheeler, T.L., Shackelford, S.D. and Koohmaraie, M. (2000). Variation in proteolysis, sarcomere length, collagen content and tenderness among major pork muscles. Journal of Animal Science. 78(4): 958-65. 

Editorial Board

View all (0)