High pressure induced changes on sarcoplasmic protein fraction and quality indicators

Meat Science

Volumn 85, Issue 1, 2010, Pages 115-120

  Marcos, Begonya ^a   Kerry, Joseph P ^b   Mullen, Anne Maria ^a  

^a ASHTOWN FOOD RESEARCH CENTRE   (Ireland)

^b UNIVERSITY COLLEGE CORK   (Ireland)

Author keywords

Beef; High pressure processing; Meat quality; Sarcoplasmic proteins

Indexed keywords

MUSCLE PROTEIN; WATER;

ANIMAL; ARTICLE; CATTLE; CHEMISTRY; COLOR; FOOD PRESERVATION; HEAT; MEAT; METHODOLOGY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRESSURE; PROTEIN DENATURATION; SARCOPLASMIC RETICULUM; SOLUBILITY; STANDARD; ANALYSIS; BOVINAE; PROCEDURES; STANDARDS;

ANIMALS; CATTLE; COLOR; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FOOD PRESERVATION; HOT TEMPERATURE; MEAT; MUSCLE PROTEINS; PRESSURE; PROTEIN DENATURATION; SARCOPLASMIC RETICULUM; SOLUBILITY; WATER;

BOVINAE;

EID: 77049107297     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.meatsci.2009.12.014     Document Type: Article

References (35)

1. Bendall J.R., and Wismer-Pedersen J. Some properties of the fibrillar proteins of normal and watery pork muscle. Journal of Food Science 27 (1962) 145-159
2. Bendixen E. The use of proteomics in meat science. Meat science 71 1 (2005) 138-149
3. Carlez A., Veciana-Nogues T., and Cheftel J.C. Changes in colour and myoglobin of minced beef meat due to high pressure processing. Lebensmittel-Wissenschaft und-Technologie 28 5 (1995) 528-538
4. Cheah P.B., and Ledward D.A. High pressure effects on lipid oxidation in minced pork. Meat Science 43 2 (1996) 123-134
5. Cheftel J.C., and Culioli J. Effects of high pressure on meat: A review. Meat Science 46 3 (1997) 211-236
6. Farouk M.M., Wieliczko K., Lim R., Turnwald S., and MacDonald G.A. Cooked sausage batter cohesiveness as affected by sarcoplasmic proteins. Meat Science 61 1 (2002) 85-90
7. Fernández P.P., Sanz P.D., Molina-García A.D., Otero L., Guignon B., and Vaudagna S.R. Conventional freezing plus high pressure-low temperature treatment: Physical properties, microbial quality and storage stability of beef meat. Meat Science 77 4 (2007) 616-625
8. Fischer C., Hamm R., and Honikel K.O. Changes in solubility and enzymic activity of muscle glycogen phosphorylase in PSE-muscles. Meat Science 3 1 (1979) 11-19
9. Galazka V.B., Dickinson E., and Ledward D.A. Influence of high pressure processing on protein solution and emulsions. Current Opinion in Colloid and Interface Science 5 (2000) 182-187
10. Goutefongea, R., Rampon, V., Nicolas, J., & Dumont, J. P. (1995). Meat color changes under high pressure treatment. In Proceedings 41st international congress of meat science and technology, 20-25 August 1995, San Antonio, Texas (pp. 384-385).
11. Gross M., and Jaenicke R. Proteins under pressure. The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes. European Journal of Biochemistry 221 (1994) 617-630
12. Jimenez Colmenero F. Muscle protein gelation by combined use of high pressure/temperature. Trends in Food Science and Technology 13 1 (2002) 22-30
13. Joo S.T., Kauffman R.G., Kim B.C., and Park G.B. The relationship of sarcoplasmic and myofibrillar protein solubility to colour and water-holding capacity in porcine longissimus muscle. Meat Science 52 3 (1999) 291-297
14. Jung S., Ghoul M., and de Lamballerie-Anton M. Influence of high pressure on the color and microbial quality of beef meat. Lebensmittel-Wissenschaft und-Technologie 36 6 (2003) 625-631
15. Kim I.J., Lee E.J., Lee N.H., Kim Y.H., and Yamamoto K. Effects of hydrostatic pressure treatment on the physicochemical, morphological, and textural properties of bovine Semitendinosus muscle. Food Science and Biotechnology 16 1 (2007) 49-54
16. Laakkonen E., Sherbon J.W., and Wellington G.H. Low-temperature, long-time heating of bovine muscle: 2. Changes in electrophoretic patterns. Journal of Food Science 35 (1970) 178-180
17. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
18. Lawrie R.A. The conversion of muscle to meat. In: Lawrie R.A. (Ed). Lawrie's Meat Science (1998), Woodhead Publishing Ltd, Cambridge 96-118
19. Lopez-Bote C., and Warriss P.D. A note on the relationships between measures of water holding capacity in the M. longissimus dorsi and total drip loss from butchered pig carcasses during storage. Meat Science 23 3 (1988) 227-234
20. Lopez-Bote C., Warriss P.D., and Brown S.N. The use of muscle protein solubility measurements to assess pig lean meat quality. Meat Science 26 3 (1989) 167-175
21. Macfarlane J.J., and McKenzie I.J. Pressure-induced solubilization of myofibrillar proteins. Journal of Food Science 41 6 (1976) 1442-1446
22. McLoughlin J.V., and Goldspink G. Post-mortem changes in the colour of pig longissimus dorsi muscle. Nature 198 (1963) 584-585
23. Messens W., Van Camp J., and Huyghebaert A. The use of high pressure to modify the functionality of food proteins. Trends in Food Science and Technology 8 4 (1997) 107-112
24. Miyaguchi Y., Nagayama K., and Tsutsumi M. Thermal and functional properties of porcine sarcoplasmic proteins: A comparison with some water-soluble animal proteins. Animal Science Journal 71 4 (2000) 416-424
25. Monin G., and Laborde D. Water holding capacity of pig muscle proteins: Interaction between the myofibrillar proteins and sarcoplasmic compounds. Science des Aliments 5 (1985) 341-345
26. Ohshima T., Ushio H., and Koizumi C. High-pressure processing of fish and fish products. Trends in Food Science and Technology 4 11 (1993) 370-375
27. Okamoto A., and Suzuki A. Effects of high hydrostatic pressure-thawing on pork meat. Trends in High Pressure Bioscience and Biotechnology, Progress in Biotechnology 19 (2002) 571-576
28. Pietrasik Z., and Shand P.J. Effect if blade tenderization and tumbling time on the processing characteristics and tenderness of injected cooked roast beef. Meat Science 66 4 (2004) 871-879
29. Ryu Y.C., Choi Y.M., and 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 71 3 (2005) 522-529
30. Sayd T., Morzel M., Chambon C., Franck M., Figwer P., Larzul C., et al. Proteome analysis of the sarcoplasmic fraction of pig Semimembranosus muscle: Implications on meat color development. Journal of Agricultural and Food Chemistry 54 7 (2006) 2732-2737
31. Sayre R.N., and Briskey E.J. Protein solubility as influenced by physiological conditions in the muscle. Journal of Food Science 28 (1963) 675-679
32. Shigehisa T., Ohmori T., Saito A., Taji S., and Hayashi R. Effects of high hydrostatic pressure on characteristics of pork slurries and inactivation of microorganisms associated with meat and meat products. International Journal of Food Microbiology 12 2-3 (1991) 207-215
33. Tornberg E. Effects of heat on meat proteins - Implications on structure and quality of meat products. Meat Science 70 3 (2005) 493-508
34. van Laack R.L.J.M., Kauffman R.G., Sybesma W., Smulders F.J.M., Eikelenboom G., and Pinheiro J.C. Is colour brightness (L-value) a reliable indicator of water-holding capacity in porcine muscle?. Meat Science 38 2 (1994) 193-201
35. Zayas J.F. Solubility of proteins. In: Zayas J.F. (Ed). Functionality of proteins in food (1997), Springer, Berlin 6-75