Diversity of meat quality of heavy pigs with respect to the rate of post-mortem glycolytic and protein changes

• Autorzy: Montowska M. , Pospiech E. , Lyczynski A. , Grzes B. , Mikolajczak B. , Iwanska E. , Kapelanski W. , Bocian M.
• Języki publikacji: EN

Abstrakty

EN

The aim of this study was to evaluate meat quality of first-farrowing sows differing in regard to the rate of post-mortem glycolytic and protein changes. Normal quality meat (RFN) (n=48) was compared with meat characterised by slower glycolytic changes (RFN-s) (n=9). The evaluation of meat quality comprised measurements of the pH value, IMP/ATP ratio, electrical conductivity, proximate composition of meat, its selected physicochemical properties and changes of proteins in centrifugal drip (2-DE and in association with Western-blotting and MALDI-TOF MS). The results showed that different acidification rate of meat modified its physico-chemical properties. The tenderness of RFN-s meat was lower than the RFN one. Mass spectrometry measurements indicate a possible association of creatine kinase with slower pH decline. Lower acidification led to a smaller thermal drip but deteriorated tenderness of meat from heavy pigs.

• Wydawca: -
• Czasopismo: Polish Journal of Food and Nutrition Sciences
• Rocznik: 2009
• Tom: 59
• Numer: 4
• Opis fizyczny: p.315-323,fig.,ref.

Twórcy

autor

Montowska M.

• Institute of Meat Technology, Poznan University of Life Sciences, Wojska Polskiego 31, 60-624 Poznan, Poland

autor

Pospiech E.

autor

Lyczynski A.

autor

Grzes B.

autor

Mikolajczak B.

autor

Iwanska E.

autor

Kapelanski W.

autor

Bocian M.

Bibliografia

• 1. Bee G., Anderson A.L., Lonergan S.M., Huff-Lonergan E., Rate and extent of pH decline affect proteolysis of cytoskeletal proteins and water-holding capacity in pork. Meat Sci., 2007, 76, 359–365.
• 2. Barbut S., Sosnicki A.A., Lonergan S.M., Knapp T., Ciobanu D.C., Gatcliffe L.J., Huff-Lonergan E., Wilson E.W., Progress in reducing the pale, soft and exudative (PSE) problem in pork and poultry meat. Meat Sci., 2008, 79, 46–63.
• 3. Berry B.W., Smith G.C., Hillers J.K., Kroening G.H., Effects of chronological age on live and carcass characteristics of Yorkshire swine. J. Anim. Sci., 1970, 31, 856–860.
• 4. Bouley J., Chambon C., Picard, B., Mapping of bovine skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry. Proteomics, 2004, 4, 1811–1824.
• 5. Candek-Potokar M., Zlender B., Lefaucheur L., Bonneau M., Effects of age and/or weight at slaughter on longissimus dorsi muscle: Biochemical traits and sensory quality in pigs. Meat Sci., 1998, 48, 287–300.
• 6. Carbonaro M., Proteomics: present and future in food quality evaluation. Trends Food Sci. Technol., 2004, 15, 209–216.
• 7. Chaze T., Bouley J., Chambon C., Barboiron C., Picard B., Mapping of alkaline proteins in bovine skeletal muscle. Proteomics, 2006, 6, 2571–2575.
• 8. Fischer Ch. Hamm R., Biochemical studies on fast glycolysing bovine muscle. Meat Sci., 1980, 4, 41–49.
• 9. Fischer K., Lindner J-P., Freudenreich P., Judas M., Höreth R., Effect of pro-longed fattening on carcass and meat quality in pigs. 2005, in: Proceedings of the 51st International Congress of Meat Science and Technology, 7 -12 August 2005, Baltimore, USA, pp. 1776–1783.
• 10. Fritz J. D., Greaser M.L., Changes in titin and nebulin in postmortem bovine muscle reveled by gel electrophoresis, western blotting and immunofluorescence microscopy. J. Food Sci., 1991, 56, 607–610, 615.
• 11. Gil M., Delday M.I., Gispert M., Font i Furnols M., Maltin Ch.M., Plastow G.S., Klont R., Sosnicki A.A., Carrión D., Relationships between biochemical characteristics and meat quality of Longissimus thoracis and Semimembranosus muscles in five porcine lines. Meat Sci., 2008, 80, 927–933.
• 12. Goll D.E., Role of proteinases and protein turnover in muscle growth and meat quality. Rec. Meat Conf. Proc., 1991, 44, 25–33.
• 13. Grześ B., Pospiech E., Koćwin–Podsiadła M., Łyczyński A., Zybert A., Mikołajczak B., Iwańska E., Analysis of the causes of meat quality variations of pigs with the genotype. Pol. J. Food Nutr. Sci., 2005, 14/55, SI 1, 59–63.
• 14. Ho C.Y., Stromer M.H., Robson R.M., Identification of the 30 kDa polypeptide in post mortem skeletal muscle as a degradation product of troponin-T. Biochimie, 1994, 76, 369–375.
• 15. Honikel K.O., Critical evaluation of methods detecting waterholding capacity in meat. 1987, in: Accelerated Processing of Meat (eds. A. Romita, C. Valin, A.A. Taylor). Elsevier App. Sci. Publ. Ltd., pp. 225–239.
• 16. Honikel K.O., Fischer Ch., A rapid method for the detection of PSE and DFD porcine muscles. J. Food Sci., 1977, 42, 1633–1636.
• 17. Huff-Lonergan E., Lonergan S.M., Mechanisms of water-holding capacity of meat: The role of postmortem biochemical and structural changes. Meat Sci., 2005, 71, 194–204.
• 18. Hwang I.H, Park B.Y., Kim J.H., Cho S.H., Lee J.M., Assessment of postmortem proteolysis by gel-based proteome analysis and its relationship to meat quality traits in pig longissimus. Meat Sci., 2005, 69, 79–91.
• 19. Jia X., Hollung K., Therkildsen M., Hildrum K.I., Bendixen E., Proteome analysis of early post-mortem changes in two bovine muscle types: M. longissimus dorsi and M. semitendinosis. Proteomics, 2006, 6, 936–944.
• 20. Joo S.T., Kauffman R.G., Kim B.C., Park G.B., The relationship of sarcoplasmic and myofibrillar protein solubility to colour and water-holding capacity in porcine longissimus muscle. Meat Sci., 1999, 52, 291–297.
• 21. Kauffman R.G., Carpenter Z.L., Bray R.W., Hoekstra W.G., Interrelations of tenderness, chronical age, and connective-tissue fraction of porcine musculature. J. Agric. Food Chem., 1964, 12, 504–507.
• 22. Koohmaraie M., Geesink G.H., Contribution of postmortem muscle biochemistry to delivery of consistent meat quality with particular focus on the calpain system. Meat Sci., 2006, 74, 34–43.
• 23. Kristensen K., Purslow P.P., The effect of ageing on the water holding capacity of pork: role of cytoskeletal proteins. Meat Sci., 2001, 58, 17–23.
• 24. Kuhn M., Beesten L., Jatsch C., Zum Einfluss der Fütterungsintensität und des Mastendgewichtes auf die Mast- und Schlachtleistung von Schweinen. 1. Mitteilung: Parameter der Mast- und Schlachtleistung, der Fleischbeschaffenheit sowie der Trockensubstanz- und Aschegehalt der Depotfette. Züchtungskunde, 1997, 69, 294–306 (in German).
• 25. Lametsch R., Roepstorff P., Bendixen E., Identification of protein degradation during post-mortem storage of pig meat. J. Agric. Food Chem., 2002, 50, 5508–5512.
• 26. Lametsch R., Karlsson A., Rosenvold K., Andersen H.J., Roepstorff P., Bendixen E., Postmortem proteome changes of porcine muscle related to tenderness. J. Agric. Food Chem., 2003, 51, 6992–6997.
• 27. Lametsch R., Roepstorff P., Møller H.S., Bendixen E., Identification of myofibrillar substrates for µ-calpain. Meat Sci., 2004, 68, 515–521.
• 28. Łyczyński A., Wajda S., Czyżak-Runowska G., Rzosińska E., Grześ B., Effect of enviromental conditions on pork meat quality – a review. Pol. J. Food Nutr. Sci., 2006, 56, 109–116.
• 29. Mikołajczak B., Pospiech E., Greaser M.L., Grześ B., Iwańska E., Łyczyński A., Two dimensional electrophoresis of proteins from centrifugal drip of various quality meat. Ann. Animal Sci., 2005, Suppl., 2, 123–126.
• 30. Morzel M., Chambon C., Hamelin M., Sante-Lhoutellier V., Sayd T., Monin G., Proteome changes during pork meat ageing following use of two different pre-slaughter handling procedures. Meat Sci., 2004, 67, 689–696.
• 31. Mullen A.M., Murray B., Troy D., Predicting the eating quality of meat. Final report. Project Armis No 4391 Agriculture Food Development Authority. National Food Centre Teagasc. Dublin, Ireland, 2000.
• 32. Mullen A.M., Stapleton P.C., Corcoran D., Hamill R.M., White A., Understanding meat quality through the application of genomic and proteomic approaches. Meat Sci., 2006, 74, 3–16.
• 33. Muroya S., Ohnishi-Kameyama M., Oe M., Nakajima I., Chikuni K., Postmortem changes in bovine troponin T isoforms on two-dimensional electrophoretic gel analyzed using mass spectrometry and western blotting: The limited fragmentation into basic polypeptides. Meat Sci., 2007, 75, 506–514.
• 34. Okumura T., Yamada R., Nishimura T., Survey of conditioning indicators for pork loins: changes in myofibrils, proteins and peptides during postmortem conditioning of vacuum-packed pork loins for 30 days. Meat Sci., 2003, 64, 467–473.
• 35. Penny I.F., Dransfeld E., Relationship between toughness and troponin T in conditioned beef. Meat Sci., 1979, 3, 135–141.
• 36. Pospiech E., Greaser M., Mikołajczak B., Szalata M., Łyczyński A., Degradation and release of titin in pork muscles. 2000, in: Proceedings 46th International Congress of Meat Science and Technology, 27 August – 1 September, Buenos Aires, Argentina, 4.I-P1, pp. 426–427.
• 37. Pospiech E., Ender K., Proteine des Fleischer als potentielle Marker der Fleischqualität. Züchtungskunde, 2006, 78, 6, 479–484 (in German).
• 38. Ryu Y.C., Choi Y.M., Kim B.C., Variations in metabolite contents and protein denaturation of the longissimus dorsi muscle in various porcine quality classifications and metabolic rates. Meat Sci., 2005, 71, 522–529.
• 39. Sárraga C., Gil M., Garcia-Regueiro J.A., Comparison of calpain and cathepsin (B, L and D) activities during dry-cured ham processing from heavy and light large white pigs. J. Sci. Food Agric., 1993, 62, 71–75.
• 40. Sawdy J.C., Kaiser S.A., St-Pierre N.R., Wick M.P., Myofibrillar loin at 36 h postmortem correlate with tenderness at 7 days. Meat Sci., 2004, 67, 421–426.
• 41. Sosnicki A.A., Pommier S., Klont R.A., Newman S., Plastow G., Best-cost production of high quality pork: bridging the gap between pig genetics, muscle biology/meat science and consumer trends. 2003, in: Proceedings of Manitoba Pork Seminar, 9–31 January,Manitoba, USA.
• 42. Strzelecki J., Borzuta K., Piechocki T., Grześkowiak E., Estimation of electrical conductivity parameters of pork various quality. Zesz. Nauk.. Przegl. Hodowl., 1995, 8 –100 (in Polish).
• 43. Strzelecki J., Lisiak D., Grześkowiak E., Borzuta K., Results of comparison of slaughter value and meat quality examinations of porkers’ carcasses from the background of selected slaughter houses in Poland and the German synthetic line BHZP-65. Roczn. Inst. Przem. Mięsn. Tłuszcz., 1999, 36, 43–51 (in Polish).
• 44. Taylor R.G.H., Geesink V.F., Thompson M., Koohmaraie M., Goll D.E., Is Z-disk degradation responsible for postmortem tenderization? J. Anim. Sci., 1995, 73, 1351–1367.
• 45. Warner R.D., Kauffman R.G., Greaser M.L., Muscle protein changes post mortem in relation to pork quality trains. Meat Sci., 1997, 45, 339–352.
• 46. Wood J.D., Enser M., Nute G.R., New feeding regimes to improve meat quality, 1995, in: Conference Proceedings International developments in process efficiency and quality in the meat industry. 16–17 November 1995, Dublin, Ireland, pp. 12–25.
• 47. Wood J.D., Jones R.C.D., Francombe M.A., Whelehan O.P., The effects of fat thickness and sex on pig meat quality with special reference to the problems associated with over leanness. 2. Laboratory and trained taste panel results. Anim. Prod., 1986, 43, 535–544.
• 48. van de Wiel D.F.M., Zhang W.L., Identification of pork quality parameters by proteomics. Meat Sci., 2007, 77, 46–54.

Uwagi

PL

Rekord w opracowaniu