Effect of pre-rigor temperature incubation on sarcoplasmic protein solubility, calpain activity and meat properties in porcine muscle

LWT

Volumn 55, Issue 2, 2014, Pages 483-489

  Liu, Jiao ^a   Ruusunen, Marita ^a   Puolanne, Eero ^a   Ertbjerg, Per ^a  

^a UNIVERSITY OF HELSINKI   (Finland)

Author keywords

Creatine kinase; Early pH decline; Glycogen phosphorylase; Sarcoplasmic protein precipitation; Water holding capacity

Indexed keywords

ENZYME ACTIVITY; MUSCLE; PHOSPHORYLATION;

CALPAINS; CREATINE KINASE; EARLY PH DECLINE; GLYCOGEN PHOSPHORYLASE; POST MORTEM; PROTEIN PRECIPITATION; PROTEIN SOLUBILITY; SARCOPLASMIC PROTEIN; SARCOPLASMIC PROTEIN PRECIPITATION; WATER-HOLDING CAPACITY;

SOLUBILITY;

SUS;

EID: 84888135971     PISSN: 00236438     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lwt.2013.10.001     Document Type: Article

References (30)

1. Bendall J.R., Wismer-Pedersen J. Some properties of the fibrillar proteins of normal and watery pork muscle. Journal of Food Science 1962, 27:144-159.
2. Borchert L.L., Powrie W.D., Briskey E.J. Astudy of the sarcoplasmic proteins of porcine muscle by starch gel electrophoresis. Journal of Food Science 1969, 34:148-152.
3. Briskey E.J., Wismer-Pedersen J. Biochemistry of pork muscle structure. 1. Rate of anaerobic glycolysis and temperature change versus the apparent structure of muscle tissue. Journal of Food Science 1961, 26:297-305.
4. Cornforth D.P., Pearson A.M., Merkel R.A. Relationship of mitochondria and sarcoplasmic reticulum to cold shortening. Meat Science 1980, 4:103-121.
5. Cross H.R., West R.L., Dutson T.R. Comparison of methods for measuring sarcomere length in beef semitendinosus muscle. Meat Science 1981, 5:261-266.
6. Dransfield E. Modeling postmortem tenderization-V: inactivation of calpains. Meat Science 1994, 37:391-409.
7. Fischer C., Hamm R., Honikel K.O. Changes in solubility and enzymic activity of muscle glycogen phosphorylase in PSE-muscles. Meat Science 1979, 3:11-19.
8. Hamm R. Kolloidchemie des Fleisches 1972, Paul Parey, Berlin and Hamburg.
9. Honikel K.O. Reference methods for the assessment of physical characteristics of meat. Meat Science 1998, 49:447-457.
10. Honikel K.O., Kim C.J., Hamm R., Roncales P. Sarcomere shortening of prerigor muscles and its influence on drip loss. Meat Science 1986, 16:267-282.
11. Jeacocke R.E. Continuous measurements of the pH of beef muscle in intact beef carcases. Journal of Food Technology 1977, 12:375-386.
12. 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 Science 1999, 52:291-297.
13. Lesiów T., Xiong Y.L. Asimple, reliable and reproductive method to obtain experimental pale, soft and exudative pork. Meat Science 2013, 93:489-494.
14. Li H., Thompson V.F., Goll D.E. Effects of autolysis on properties of μ- and m-calpain. Biochimica et Biophysica Acta (BBA)-Molecular Cell Research 2004, 1691:91-103.
15. Melody J.L., Lonergan S.M., Rowe L.J., Huiatt T.W., Mayes M.S., Huff-Lonergan E. Early postmortem biochemical factors influence tenderness and water-holding capacity of three porcine muscles. Journal of Animal Science 2004, 82:1195-1205.
16. Offer G., Knight P. The structural basis of water-holding in meat. Part 2: drip losses. Developments in meat science 1988, Vol. 4:173-241. Elsevier Applied Science, London.
17. Offer G., Trinick J. On the mechanism of water holding in meat: the swelling and shrinking of myofibrils. Meat Science 1983, 8:245-281.
18. Pomponio L., Ertbjerg P. The effect of temperature on the activity of μ- and m-calpain and calpastatin during post-mortem storage of porcine longissimus muscle. Meat Science 2012, 91:50-55.
19. Pomponio L., Ertbjerg P., Karlsson A.H., Costa L.N., Lametsch R. Influence of early pH decline on calpain activity in porcine muscle. Meat Science 2010, 85:110-114.
20. Pomponio L., Lametsch R., Karlsson A.H., Costa L.N., Grossi A., Ertbjerg P. Evidence for post-mortem m-calpain autolysis in porcine muscle. Meat Science 2008, 80:761-764.
21. Puolanne E., Halonen M. Theoretical aspects of water-holding in meat. Meat Science 2010, 86:151-165.
22. Rhee M.S., Ryu Y.C., Kim B.C. Postmortem metabolic rate and calpain system activities on beef longissimus tenderness classifications. Bioscience, Biotechnology, and Biochemistry 2006, 70:1166-1172.
23. 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 Science 2005, 71:522-529.
24. Schäfer A., Rosenvold K., Purslow P.P., Andersen H.J., Henckel P. Physiological and structural events post mortem of importance for drip loss in pork. Meat Science 2002, 61:355-366.
25. Scopes R.K. The influence of post-mortem conditions on the solubilities of muscle proteins. Biochemical Journal 1964, 91:201-207.
26. Sierra V., Fernández-Suárez V., Castro P., Osoro K., Vega-Naredo I., García-Macía M., et al. Identification of biomarkers of meat tenderisation and its use for early classification of Asturian beef into fast and late tenderising meat. Journal of the Science of Food and Agriculture 2012, 92:2727-2740.
27. Van Laack R.L.J.M., Kauffman R.G. Glycolytic potential of red, soft, exudative pork longissimus muscle. Journal of Animal Science 1999, 77:2971-2973.
28. Warner R.D., Kauffman R.G., Greaser M.L. Muscle protein changes post mortem in relation to pork quality traits. Meat Science 1997, 45:339-352.
29. Zhu X., Ruusunen M., Gusella M., Ylä-Ajos M., Xu X., Zhou G., et al. High early post-mortem temperature induces activation of AMP-activiated protein kinase and development of pale, soft and exudative characteristics in turkey muscles. Meat Science 2013, 93:600-606.
30. Zhu X., Ruusunen M., Gusella M., Zhou G., Puolanne E. High post-mortem temperature combined with rapid glycolysis induces phosphorylase denaturation and produces pale and exudative characteristics in broiler Pectoralis major muscles. Meat Science 2011, 89:181-188.