Hostname: page-component-cd9895bd7-7cvxr Total loading time: 0 Render date: 2024-12-18T17:06:24.490Z Has data issue: false hasContentIssue false
  • English
  • Français

Understanding tenderness variability and ageing changes in buffalo meat: biochemical, ultrastructural and proteome characterization

Published online by Cambridge University Press:  06 January 2016

M. Kiran ,
B. M. Naveena ,
K. S. Reddy ,
M. Shahikumar ,
V. R. Reddy ,
V. V. Kulkarni ,
S. Rapole  and
T. H. More
M. Kiran*
Affiliation:
Department of Livestock Products Technology, College of Veterinary Sciences, Hyderabad 500030, India
B. M. Naveena
Affiliation:
National Research Centre on Meat, Chengicherla, Hyderabad 500092, India
K. S. Reddy
Affiliation:
Department of Livestock Products Technology, College of Veterinary Sciences, Hyderabad 500030, India
M. Shahikumar
Affiliation:
Department of Livestock Products Technology, College of Veterinary Sciences, Hyderabad 500030, India
V. R. Reddy
Affiliation:
Department of Livestock Products Technology, College of Veterinary Sciences, Hyderabad 500030, India
V. V. Kulkarni
Affiliation:
National Research Centre on Meat, Chengicherla, Hyderabad 500092, India
S. Rapole
Affiliation:
Proteomics Lab, National Centre for Cell Science, Pune 411007, India
T. H. More
Affiliation:
Proteomics Lab, National Centre for Cell Science, Pune 411007, India
*
†E-mail: [email protected]
Get access

Abstract

Understanding of biological impact of proteome profile on meat quality is vital for developing different approaches to improve meat quality. Present study was conducted to unravel the differences in biochemical, ultrastructural and proteome profile of longissimus dorsi muscle between buffaloes (Bubalus bubalis) of different age groups (young v. old). Higher (P<0.05) myofibrillar and total protein extractability, muscle fibre diameter, and Warner-Bratzler shear force (WBSF) values was observed in old buffalo meat relative to meat from young buffaloes. Scanning electron microscopy photographs revealed reduced fibre size with increased inter-myofibrillar space in young compared with old buffalo meat. Transmission electron microscopy results revealed longer sarcomeres in young buffalo meat relative to meat from old buffaloes. Proteomic characterization using two-dimensional gel electrophoresis (2DE) found 93 differentially expressed proteins between old and young buffalo meat. Proteome analysis using 2DE revealed 191 and 95 differentially expressed protein spots after 6 days of ageing in young and old buffalo meat, respectively. The matrix assisted laser desorption ionization time-of flight/time-of flight mass spectrometry (MALDI-TOF/TOF MS) analysis of selected gel spots helped in identifying molecular markers of tenderness mainly consisting of structural proteins. Protein biomarkers identified in the present study have the potential to differentiate meat from young and old buffaloes and pave the way for optimizing strategies for improved buffalo meat quality.

Keywords

buffalo meatproteomicsmass spectrometrytendernessultrastructure
Type
Research Article
Information
animal , Volume 10 , Issue 6 , June 2016 , pp. 1007 - 1015
Copyright
© The Animal Consortium 2016 

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

Anjaneyulu, ASR, Sengar, SS, Lakshmanan, V and Joshi, BC 1985. Meat quality of male buffalo calves maintained in different levels of protein. Buffalo Bulletin 4, 44–47.Google Scholar
Anjaneyulu, ASR, Sharma, N and Kondaiah, N 1989. Evaluation of salt, polyphosphates and their blends at different levels on physicochemical properties of buffalo meat and patties. Meat Science 25, 293–306.Google Scholar
AOAC 2005. Official methods of analysis. Association of Official Analytical Chemists, Washington, DC.Google Scholar
Bjarnadottir, SG, Hollung, K, Færgestad, EM and Veiseth-Kent, E 2010. Proteome changes in bovine longissimus thoracis muscle during the first 48h postmortem: Shifts in energy status and myofibrillar stability. Journal of Agriculture and Food Chemistry 58, 7408–7414.Google Scholar
Bjarnadottir, SG, Hollung, K, Hoy, M, Bendixen, E, Codrea, MC and Veiseth-Kent, E 2012. Changes in protein abundance between tender and tough meat from bovine longissimus thoracis muscle assessed by isobaric Tag for Relative and Absolute Quantitation (iTRAQ) and 2-dimensional gel electrophoresis analysis. Journal of Animal Science 90, 2035–2043.Google Scholar
Bouley, J, Chambon, C and Picard, B 2004. Mapping of bovine skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry. Proteomics 4, 1811–1824.Google Scholar
Bozzola, JJ and Russell, LD 1998. Electron microscopy principles and techniques for biologists, 2nd edition. Jones and Bartlett Publishers, Sudbury, Massachusetts. pp. 19–67.Google Scholar
Flower, TR, Chesnokova, LS, Froelich, CA, Dixon, C and Witt, SN 2005. Heat shock prevents alpha-synuclein-induced apoptosis in a yeast model of Parkinson’s disease. Journal of Molecular Biology 351, 1081–1100.Google Scholar
Gagaoua, M, Boudida, Y, Becila, S, Picard, B, Boudjellal, A, Sentandreu, MA and Ouali, A 2012. New caspases inhibitors belonging to the serpin superfamily: A novel key control point of apoptosis in mammalian tissues. Advances in Bioscience and Biotechnology 3, 740–750.Google Scholar
Gerelt, B, Ikeuchi, Y, Nishiumi, T and Suzuki, A 2002. Meat tenderization by calcium chloride after osmotic dehydration. Meat Science 60, 237–244.Google Scholar
Hawkins, RR, Davis, GW, Cable, JK Jr and Ramsey, CB 1987. Fragmentation index as an early postmortem predictor of beef tenderness. Journal of Animal Science 64, 171–176.Google Scholar
Hollung, K, Grove, H, Faergestad, EM, Sidhu, MS and Berg, P 2009. Comparison of muscle proteome profiles in pure breeds of Norwegian Landrace and Duroc at three different ages. Meat Science 81, 487–492.Google Scholar
Jia, X, Hollung, K, Therkildsen, M, Hildrum, KI and Bendixen, E 2006. Proteome analysis of early post-mortem changes in two bovine muscle types: M. longissimus dorsi and M. semitendinosis. Proteomics 6 (3), 936–944.Google Scholar
Joo, ST, Kauffman, RG, Kim, BC and Park, GB 1999. The relationship of sarcoplasmic and myofibrillar protein solubility to colour and water holding capacity in porcine longissimus muscle. Meat Science 35, 276–278.Google Scholar
Kandeepan, G, Anjaneyulu, ASR, Kondaiah, N, Mendiratta, SK and Lakshmanan, V 2009. Effect of age and gender on the processing characteristics of buffalo meat. Meat Science 83, 10–14.Google Scholar
Keshava Rao, V, Anjaneyulu, ASR, Lakshmanan, V, Sharma, N and Kondaiah, N 1985. Meat and fat characteristics of male buffalo calves. Indian Journal of Animal Science 55, 596–598.Google Scholar
Kim, NK, Cho, S, Lee, SH, Park, HR, Lee, CS, Cho, YM, Choy, YH, Yoon, D, Im, SK and Park, EW 2008. Proteins in longissimus muscle of Korean native cattle and their relationship to meat quality. Meat Science 80, 1068–1073.Google Scholar
Lametsch, R, Karlsson, A, Rosenvold, K, Andersen, HJ, Roepstorff, P and Benedixen, E 2003. Postmortem proteome changes of porcine muscle related to tenderness. Journal of Agriculture and Food Chemistry 51, 6992–6997.Google Scholar
Lapitan, RM, Delbarrio, AN, Katsube, O, Ban-Tokuda, T, Orden, EA, Robles, AY, Fujihara, T, Cruz, LR, Homma, H and Kannai, Y 2007. Comparison of carcass and meat characteristics of Brahman grade cattle (Bos indicus) and crossbred water buffalo (Bubalus bubalis). Journal of Animal Science 78, 599–604.Google Scholar
Laville, E, Sayd, T, Morzel, M, Blinet, S, Chambon, C, Lepetit, J, Renand, G and Hocquette, JF 2009. Proteome changes during meat aging in tough and tender beef suggest the importance of apoptosis and protein solubility for beef aging and tenderization. Journal of Agriculture and Food Chemistry 57, 10755–107641.Google Scholar
Lawrie, R 1998. Lawrie’s meat science, 6th edition. Woodhead Publishing Ltd, Cambridge, England.Google Scholar
Marino, R, Albenzio, M, della Malva, A, Santillo, A, Loizzo, P and Sevi, A 2013. Proteolytic pattern of myofibrillar protein and meat tenderness as affected by breed and aging time. Meat Science 95, 281–287.CrossRefGoogle ScholarPubMed
Monson, F, Sanudo, C and Sierra, I 2005. Influence of breed and ageing time on the sensory meat quality and consumer acceptability in intensively reared beef. Meat Science 71 (3), 471–479.Google Scholar
Naveena, B M, Kiran, M, Sudhakar Reddy, K, Ramakrishna, C, Vaithiyanathan, S and Devatkal, SK 2011. Effect of ammonium hydroxide on ultrastructure and tenderness of buffalo meat. Meat Science 88, 727–732.Google Scholar
Naveena, B M, Mendiratta, SK and Anjaneyulu, ASR 2004. Tenderization of buffalo meat using plant protease from Cucumis trigonus ruxb (Kachri) and Zingiber officinale roscoe (Ginger rhizome). Meat Science 68, 363–369.Google Scholar
Neath, KE, Del Barrio, AN, Lapitan, RM, Herrera, J R V, Cruz, L C, Fujihara, T, Muroya, S, Chikuni, K, Hirabayashi, M and Kanai, Y 2007. Difference in tenderness and pH decline between water buffalo meat and beef during postmortem aging. Meat Science 75, 499–505.Google Scholar
Ouali, A, Gagaoua, M, Boudida, Y, Becila, S, Boudjellal, A, Herrera-Mendez, CH and Sentandreu, MA 2013. Biomarkers of meat tenderness: present knowledge and perspectives in regards to our current understanding of the mechanisms involved. Meat Science 95, 854–870.CrossRefGoogle ScholarPubMed
Polati, R, Menini, M, Robotti, E, Millioni, R, Marengo, E, Novelli, E, Balzan, S and Cecconi, D 2012. Proteomic changes involved in tenderization of bovine longissimus dorsi muscle during prolonged ageing. Food Chemistry 135, 2052–2069.Google Scholar
Sahoo, J and Anjaneyulu, ASR 2000. Effect of sodium ascorbate, alpha-tocopherol acetate and sodium tripolyphosphate on the quality of pre blended ground buffalo meat. Journal of Food Science and Technology 37, 388–393.Google Scholar
Sentandreu, MA, Coulis, G and Ouali, A 2002. Role of muscle endopeptidases and their inhibitors in meat tenderness. Trends in Food Science and Technology 13, 400–421.Google Scholar
Shevchenko, A, Wilm, M, Vorm, O and Mann, M 1996. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Analytical Chemistry 68, 850–858.Google Scholar
Singh, UB and Sulochana, MB 1977. Handbook of histological and histochemical techniques, 2nd edition. Premier Publishing House, Hyderabad, India.Google Scholar
Spurr, AR 1969. A low-viscosity epoxy resin embedding medium for electron microscopy. Journal of Ultrastructure Research 26, 31–43.Google Scholar
Syed Ziauddin, K, Mahendrakar, NS, Rao, DN, Ramesh, BS and Amla, BL 1994. Observations on some chemical and physical characteristics of buffalo meat. Meat Science 37, 103–113.Google Scholar
Tepas, MW, Jansen, J, Konrad, CJ, Broekman, A, Henny, R and Heuven, HCM 2008. Post mortem proteome degradation profiles of longissimus muscle in Yorkshire and Duroc. Archiv Tierzucht 51, 62–68.Google Scholar
Trout, GR 1989. Variation in myoglobin denaturation and color of cooked beef, pork and turkey meat as influenced by pH, sodium chloride, sodium tripolyphosphate, and cooking temperatures. Journal of Food Science 54, 536–544.CrossRefGoogle Scholar
Tuma, HJ, Venable, JH, Wuthier, PR and Henrickson, RL 1962. Relationship of fibre diameter to tenderness and meatiness as influenced by bovine age. Journal of Animal Science 21, 33–36.Google Scholar
Valin, C, Pinkas, A, Drahnev, H, Boikovski, S and Polikronov, D 1984. Comparative study of buffalo meat and beef. Meat Science 10, 69–84.Google Scholar
Vieira, C, Cerdeño, A, Seffano, E, Lavín, P and Mantecón, AR 2007. Breed and ageing extent on carcass and meat quality of beef from adult steers (oxen). Livestock Science 107, 62–69.Google Scholar
Wardlaw, FB, Maccaskill, LH and Acton, JC 1973. Effect of postmortem muscle changes in poultry meat loaf properties. Journal of Food Science 38, 421–424.Google Scholar
Warris, PD 1979. The extraction of haem pigments from fresh meat. Journal of Food Technology 14, 75–80.CrossRefGoogle Scholar
Wheeler, TD 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.CrossRefGoogle ScholarPubMed
Zapata, I, Zerby, HN and Wick, M 2009. Functional proteomic analysis predicts beef tenderness and the tenderness differential. Journal of Agriculture and Food Chemistry 57, 4956–4963.Google Scholar
Zapata, I, Reddish, JM, Miller, MA, Lilburn, MS and Wick, M 2012. Comparative proteomic characterization of the sarcoplasmic proteins in the pectoralis major and supracoracoideus breast muscles in 2 chicken genotypes. Poultry Science 91, 1654–1659.Google Scholar