Ultra-fast freezing and low storage temperatures are not necessary to maintain the functional properties of manufacturing beef

Meat Science

Volumn 66, Issue 1, 2004, Pages 171-179

  Farouk, M M ^a   Wieliczko, K J ^a   Merts, I ^a  

^a RUAKURA RESEARCH CENTRE   (New Zealand)

Author keywords

Beef; Freezing rate; Functional properties; Muscle type; Storage temperature

Indexed keywords

FREEZING; HYDROPHOBICITY; MUSCLE; PROTEINS;

BLAST FREEZING;

MEATS;

EID: 0041355270     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0309-1740(03)00081-0     Document Type: Article

References (50)

1. Akamittath, J. G., Brekke, C. J., & Schanus, E. G. (1990). Lipid oxidation and color stability in restructured meat systems during frozen storage. Journal of Food Science, 55, 1513-1517.
2. Anon (1986). Effect of freezing rate, storage temperature, temperature abuse and storage time on sensory, chemical, instron and yield properties of beef roast. Report prepared for US Army Natick Research and Development Laboratories Natick, Massachusetts 01760.
3. Aňón, M. C., & Calvelo, A. (1980). Freezing rate effects on the drip loss of frozen beef. Meat Science, 4, 1-14.
4. Awad, A., Powrie, W. D., & Fennema, O. (1968). Chemical deterioration of frozen muscle. Journal of Food Science, 33, 227-234.
5. Berry, B. W., & Leddy, K. F. (1989). Effect of freezing rate, frozen storage temperature and storage time on tenderness values of beef patties. Journal of Food science, 54, 291-296.
6. Boles, J. A., & Swan, J. E. (1996). Effect of post-slaughter processing and freezing on the functionality of hot-boned meat from young bull. Meat Science, 44, 11-18.
7. Braggins, T. J., Frost, D. A., Agnew, M. P., & Podmore, C. (1999). Changes in pH and free amino acids in sheepmeat during extended chilled storage. Proceedings 45th International Conference of Meat Science & Technology. Yokohama, Japan.
8. Brake, N. C., & Fennema, O. R. (1999). Glass transition values of muscle tissue. Journal of Food Science, 64, 10-15.
9. Butkus, H. (1970). Accelerated denaturation of myosin in frozen solution. Journal of Food Science, 35, 558-562.
10. Crouse, J. D., & Koohmaraie, M. (1990). Effect of freezing of beef on subsequent post-mortem aging and shearforce. Journal of Food Science, 55, 573-574.
11. Davey, C. L. (1960). The effect of carnosine and anserine on glycolytic reactions in skeletal muscle. Archives of Biochemistry and Biophysics, 89, 296-302.
12. Ellman, G. L. (1959). Tissue sulfhydryl groups. Archives of Biochemistry and Biophysics, 82, 70-77.
13. Farouk, M. M., Hall, W. K., & Swan, J. E. (2000). Attributes of beef sausage batters, patties and restructured roasts from two boning systems. Journal of Muscle Foods, 11, 197-212.
14. Farouk, M. M., & Swan, J. E. (1997). Effect of pH at time of salting on the functional properties of pre-rigor beef. Meat Science, 45, 463-472.
15. Farouk, M. M., & Swan, J. E. (1998a). Effect of rigor temperature and frozen storage on functional properties of hot-boned manufacturing beef. Meat Science, 49, 233-247.
16. Farouk, M. M., & Swan, J. E. (1998b). Effect of muscle condition before freezing and simulated chemical changes during frozen storage on the pH and colour of beef. Meat Science, 50, 245-256.
17. Farouk, M. M., & Wieliczko, K. J. (2002). Effect of diet and fat content on the functional properties of thawed beef. Meat Science (in press).
18. Franks, F. (1995). Protein destabilization at low temperatures. Advances in Protein Chemistry, 46, 105-139.
19. Genstat. (1993). Genstat 5, Release 3, Reference Manual. UK: Oxford University Press.
20. Grau, R., & Hamm, R. (1953). Eine einfache Methode zur Bestimmung der Wasserbindung im Muskel. Naturwissenschaften, 40, 29-30.
21. Grau, R., & Hamm, R. (1957). Über das Wassesbindungsvermögen des Säugetiermuskels. II Mitt. Über die Bestimmung der Wasserbindung des Muskels. Z. Lebensm. Untersuch._Forsch., 105, 446_460.
22. Grujiæ, R., Petroviæ, L., Pikula, B., & Amidžiæ, L. (1993). Definition of the Optimum freezing rate - 1. Investigation of structure and ultrastructure of beef m. longissimus dorsi frozen at different freezing rates. Meat Science, 33, 301-318.
23. Henrickson, R. L., & Asghar, A. (1985). Cold storage energy aspect of electrically stimulated hot-boned meat. In A. M. Pearson, & T. R. Dutson (Eds.), Advances in meat research (Vol. 1) (pp. 237). Wesport, CT. USA: Avi Publishing Co., Inc.
24. Hertzman, C., Olsson, U., & Tornberg, E. (1993). The influence of high temperature, type of muscle and electrical stimulation on the course of rigor, ageing and tenderness of beef muscles. Meat Science, 35, 119-141.
25. Hunt, M. C., & Hedrick, H. B. (1977). Profile of fiber types and related properties of five bovine muscles. Journal of Food Science, 42, 513-517.
26. IIR. (1972). Recommendations for the processing and handling of frozen foods (2nd ed.). Paris: International Institute of Refrigeration.
27. Khan, A. W., & Lentz, C. P. (1977). Effects of freezing, thawing and storage on some quality factors for portion-size beef cuts. Meat Science, 1, 263-270.
28. Ledward, D. A. (1985). Post-slaughter influences on the formation of metmyoglobin in beef muscles. Meat Science, 15, 149-171.
29. Li-Chan, E., Nakai, S., & Wood, D. F. (1985). Relationship between functional (fat binding, emulsifying) and physicochemical properties of muscle proteins. Effects of heating, freezing, pH and species. Journal of Food Science, 50, 1034-1040.
30. Lin, T. M., & Park, J. W. (1998). Solubility of salmon myosin as affected by conformational changes at various ionic strengths and pH. Journal of Food Science, 63, 215-218.
31. Lindeløv, F. (1978). Reactions in frozen foods; the reactions of myosin and single amino acids with some aldehydes. International Journal of Refrigeration, 1(2), 92-98.
32. Liu, Q., Scheller, K. K., Arp, S. C., Schaefer, D. M., & Frigg, M. (1996). Color coordinates for assessment of dietary vitamin E. Effects on beef color stability. Journal of Animal Science, 74, 106-116.
33. Matsumoto, J. J. (1979). Denaturation of fish proteins during frozen storage. In O. Fennema (Ed.), Proteins at low temperatures. Advances in Chemistry Series 180 (pp. 205-224). Washington, DC: American Chemical Society.
34. Miller, A. J., Ackerman, S. A., & Palumbo, S. A. (1980). Effects of frozen storage on functionality of meat for further processing. Journal of Food Science, 45, 1466-1471.
35. Mittal, G. S., & Barbut, S. (1991). Effects of freezing rate and storage time on the structural properties of minced meat. Lebensmittel-Wissenschaft- und- Technologie, 24, 226-230.
36. Ngapo, T. M., Babare, I. H., Reynolds, J., & Mawson, R. F. (1999a). Freezing rate and frozen storage effects on the ultrastructure of samples of pork. Meat Science, 53, 159-168.
37. Ngapo, T. M., Babare, I. H., Reynolds, J., & Mawson, R. F. (1999b). Freezing and thawing rate effects on drip loss from samples of pork. Meat Science, 53, 149-158.
38. Pearce, K. N., & Kinsella, J. E. (1978). Emulsifying properties of proteins: evaluation of a turbidimetric technique. Journal of Agricultural Food Chemistry, 26, 716-723.
39. Petrović, L., Grujić, R., & Petrović, M. (1993). Definition of the optimum freezing rate - 2. Investigation of the physico-chemical properties of beef m. longissimus dorsi frozen at different freezing rates. Meat Science, 33, 319-331.
40. Puolanne, E., & Turkki, P. (1985). The effect of freeze storage on the water binding capacity of the raw materials of cooked sausage. Proceedings of European Meeting of Meat Research Workers No. 31, 583-586.
41. Rahelić, S., Gawwad, A. H., & Puač, S. (1985). Structure of beef longissimus dorsi muscle frozen at various temperatures: Part 2 - ultrastructure of muscles frozen at -10, -22, -33, -78 and -115 °C. Meat Science, 14, 73-81.
42. Reid, D. S. (1999). Factors which influence the freezing process an examination of new insights. Paper presented at the 20th International Congress of Refrigeration, IIR/IIF, Sydney.
43. Sebranek, J. G., Sang, P. N., Topel, D. G., & Rust, R. E. (1979). Effects of freezing methods and frozen storage on chemical characteristics of ground beef patties. Journal of Animal Science, 4, 1101-1108.
44. Seideman, S. C., Cross, H. R., Smith, G. C., & Durland, P. R. (1984). Factors associated with fresh meat color: a review. Journal of Food Quality, 6, 211-237.
45. Shenouda, S. Y. K. (1980). Theories of protein denaturation during frozen storage of fish flesh. Advances in Food Research, 26, 275-311.
46. Slade, L., & Levine, H. (1991). Beyond water activity: recent advances on an alternative approach to the assessment of food quality and safety. Critical Review Food Science and Nutrition, 30(2-3), 115-360.
47. Tomás, M. C., & Aňón, M. C. (1990). Study on the influence of freezing rate on lipid oxidation in fish (salmon) and chicken breast muscles. International Journal of Food Science and Technology, 25, 718-721.
48. Wagner, J. R., & Aňón, M. C. (1985). Effect of freezing rate on the denaturation of myofibrillar proteins. Journal of Food Technology, 20, 735-744.
49. Wagner, J. R., & Aňón, M. C. (1986a). Effect of frozen storage on protein denaturation in bovine muscle 1. Myofibrillar ATPase activity and differential scanning calorimetric studies. Journal of Food Technology, 21, 9-18.
50. Wagner, J. R., & Aňón, M. C. (1986b). Effect of frozen storage on protein denaturation in bovine muscle. II. Influence on solubility, viscosity and electrophoretic behaviour of myofibrillar proteins. Journal of Food Technology, 21, 547-558.