Application of high hydrostatic pressure to meat and meat processing

Advanced Technologies for Meat Processing

Volumn , Issue , 2006, Pages 193-218

  Suzuki, Atsushi ^a   Kim, Ken ^a   Tanji, Hiroyuki ^a   Nishiumi, Tadayuki ^a   Ikeuchi, Yoshihide ^b  

^a NIIGATA UNIVERSITY   (Japan)

^b KYUSHU UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CULTIVATION; FORESTRY; HIGH PRESSURE ENGINEERING; HYDRAULICS; HYDROSTATIC PRESSURE; MEATS; PROCESSED FOODS;

EGG ALBUMEN; FOOD MATERIALS; HEAT PROCESSING; HIGH HYDROSTATIC PRESSURE; HIGH PRESSURE; HIGH PRESSURE TECHNOLOGY; MASS CULTIVATION; MEAT PROCESSING;

THERMAL PROCESSING (FOODS);

EID: 85010767743     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter

References (96)

1. Anderson, T. J., and F. C. Parrish, Jr. 1989. Postmortem degradation of titin and nebulin of beef steaks varying in tenderness. J. Food Sci. 54: 748-749
2. Asghar, A., K. Samejima, and T. Yasui. 1985. Functionality of muscle proteins in gelation mechanism of structured meat products. CRC Critical Reviews in Food Science and Nutrition. 22: 27-106
3. Baines, D., and J. Mlotkiewicz. 1984. The chemistry of meat flavor. In Recent advances in the chemistry of meat, ed. A. J. Bailey, 119-164. London: Royal Society of Chemistry.
4. Beilken, S. L., J. J. Macfarlane, and P. N. Jones. 1990. Effects of high pressure during heat treatment on theWarner-Blatzler shear force values of selected beef muscles. J. Food Sci. 55: 15-18, 42.
5. Bouton, P. E., A. L. Ford, P. V. Harris, J. J. Macfarlane, and J. M. O’Shea. 1977. Pressureheat treatment of post-rigor muscle: Effect on tenderness. J. Food Sci. 42: 132-135
6. Bridgman, P. W. 1914. The coagulation of albumen by pressure. J. Biol. Chem. 19: 511-512
7. Calkins, C. R., and G. W. Davis. 1980. Fragmentation index of raw muscle as a tenderness predictor of steaks from good and standard steer and bullock carcasses. J. Anim. Sci. 55: 1067-1072
8. Carlez, A., T. Veciana-Nugues, and J. C. Cheftel. 1995. Changes in colour and myoglobin of minced beef meat due to high pressure processing. Lebensm-Wiss Technol. 28: 528-538
9. Cheah, P. B., and D. A. Ledward. 1996. High pressure effects on lipid oxidation in minced pork. Meat Sci. 43: 123-134
10. Cheah, P. B., and D. A. Ledward. 1997. Inhibition of metmyoglobin formation in fresh beef by pressure treatment. Meat Sci. 45: 411-418
11. Cheftel, J. 1992. Effects of high hydrostatic pressure on food constituents: An overview. In High pressure and biotechnology, eds. C. Balny, R. Hayashi, K. Heremans, and P. Masson, 195-209. Montrouge: John Libbey Eurotext.
12. Cheftel, J. C. 1995. Review: High-pressure, microbial inactivation and food preservation. Food Sci. Technol. Intern. 1: 75-90
13. Cheftel, J. C., and J. Culioli. 1997. Effects of high pressure on meat: A review. Meat Sci. 46: 211-236
14. Cheftel, J. C., J. Levy, and D. Dumay. 2000. Pressure-assisted freezing and thawing: Principles and potential applications. Food Rev. Int. 16: 453-483
15. Cheftel, J. C., M. Thiebaud, and E. Dumay. 2002. Pressure-assisted thawing and freezing of foods: A review of recent studies. High Pressure Res. 22: 601-611
16. Cheftel, J. C., M. Thiebaud, and E. Dumay. 2003. High pressure-low temperature processing of foods: A review. In Advances in high pressure and biotechnology, ed. R. Winter, 327-340. Berlin: Springer.
17. Davey, C. L., and K. V. Gilbert. 1967. Structural changes in meat during ageing. J. Food Technol. 2: 57-59
18. de Lambellerie-Anton, E. M., R. G. Taylor, and J. Culioli. 2002. High pressure processing of meat. In Meat processing: Improving quality, eds. J. Kerry, J. Kerry, and D. A. Ledward, 313-331. Boca Raton, FL: CRC/Wood Head.
19. Defaye, A., D. A. Ledward, D. A. MacDougall, and R. F. Tester. 1995. Renaturation of metmyoglobin subjected to high isostaticpressure. Food Chem. 52: 19-22
20. Elgasim, E. A., and W. H. Kennick. 1982. Effect of high pressure on meat microstructure. Food Microstruct. 1: 75-82
21. Fukazawa, T., and T. Yasui. 1967. The changes in the zigzag configuration of the Z-line of myofibrils. Biochim. Biophys. Acta. 140: 534-537
22. Furst, D. O., M. Osborn, R. Nave, and K. Weber. 1988. The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: A map of ten repetitive epitopes starting at the Z line extends close to the M line. J Cell. Biol. 106: 1563-1572
23. Grebol, N. 2002. Commercial use of high hydrostatic pressure in sliced cooked ham in Spain. In Trends in high pressure bioscience and technology, ed. R. Hayashi, 385-388. Amsterdam: Elsevier Science.
24. Hayashi, R. 1992. Utilization of pressure in addition to temperature in food science and technology. In High pressure and biotechnology, eds. C. Balny, R. Hayashi, K. Heremans, and P. Masson, 185-193. Montrouge: John Libbey Eurotext.
25. Homma, N., Y. Ikeuchi, and A. Suzuki. 1994. Effects of high-pressure treatment on the proteolytic enzymes in meat. Meat Sci. 38: 219-228
26. Horowits, R., E. S. Kempner, M. E. Bisher, and R. J. Podolsky. 1986. A physiological role for titin and nebulin in skeletal muscle. Nature. 323: 160-164
27. Ikeuchi, Y., H. Tanji, K. Kim, and A. Suzuki. 1992a. Dynamic rheological measurements on heat-induced pressurized actomyosin gels. J. Agric. Food Chem. 40: 1751-1755
28. Ikeuchi, Y., H. Tanji, K. Kim, and A. Suzuki. 1992b. Mechanism of heat-induced gelation of pressurized actomyosin: Pressure-induced changes in actin and myosin in actomyosin. J. Agric. Food Chem. 40: 1756-1761
29. Ikkai, T., and T. Ooi. 1966. The effects of pressure on G-F transformation of actin. Biochem. 5: 1551-1560
30. Ikkai, T., and T. Ooi. 1969. The effects of pressure on actomyosin systems. Biochem. 8: 2615-2622
31. Ishioroshi, M., K. Samejima, and T. Yasui. 1983. Heat-induced gelation of myosin filaments at a low concentration. Agric. Biol. Chem. 47: 2809-2816
32. Ivanov, I., Y. N. Bert, and N. A. Lebedeva. 1960. Changes in some properties of myosin, actomyosin and actin under the influence of high pressure. Biokhimiya. 25: 505-510
33. Johnston, D. J. 1995. High pressure effects on milk and meat. In High pressure processing of foods, eds. D. A. Edward, D. E. Johnston, R. G. Earnshaw, and A. P. M. Hasting, 99-121. Nottingham, UK: Nottingham University Press.
34. Josephs, R., and W. F. Harrington. 1966. Studies on the formation and physical chemical properties of synthetic myosin filaments. Biochem. 5: 3474-3487
35. Josephs, R., and W. F. Harrington. 1967. An unusual pressure dependence for a reversibly associating protein system: Sedimentation studies on myosin. Proc. Natl. Acad. Sci. USA. 58: 1587-1594
36. Josephs, R., and W. F. Harrington. 1968. On the stability of myosin filaments. Biochem. 7: 2834-2845
37. Jung, S., E. M. de Lamballerie-Anton, R. G. Taylor, and M. Ghouk. 2000. High pressure effects on lysosome integrity and lysosomal enzyme activity in bovine muscle. J. Agric. Food Chem. 48: 2467-2471
38. Kennick, W. H., E. A. Elgasim, Z. A. Holmes, and P. F. Meyer. 1980. The effect of pressurization of pre-rigor muscle on post-mortem meat characteristics. Meat Sci. 4: 33-40
39. Kim, K., Y. Homma, Y. Ikeuchi, and A. Suzuki. 1993. Effect of high hydrostatic pressure on the conversion of α-connectin to β-connectin. J. Biochem. 114: 463-467
40. Kim, K., Y. Homma, Y. Ikeuchi, and A. Suzuki. 1995. Cleavage of connectin by calpain and cathepsin D. Biosci. Biotech. Biochem. 59: 896-899
41. Kimura, S., T. Matsumura, S. Ohtsuki, Y. Nakauchi, A. Matsuno, and K. Maruyama. 1992. Characterization and localization of α-connectin(titin 1): An elastic protein isolated from rabbit skeletal muscle. J. Muscle Res. Cell Motil. 13: 39-47
42. Kinsella, J. E., and D. M. Whitehead. 1989. Protein in whey: Chemical, physical and functional properties. Adv. Food. Nutr. Res. 33: 343-438
43. Knorr, D. 1996. Advantages, opportunities and challenges of high hydrostatic pressure application to food systems. In High pressure bioscience and biotechnology, eds. R. Hayashi and C Balny, 279-287. Amsterdam: Elsevier Science.
44. Ko, W. C., M. Tanaka, Y. Nagashima, T. Taguchi, and K. Amano. 1990. Effect of high pressure treatment on the thermal gelation of sardine and Alaska pollack meat and myosin paste. Nippon Shokuhin Kogyo Gakkaishi. 37: 637-642
45. Locker, R. H., and D. J. C. Wild. 1984. Tenderization of meat by pressure-heat involves weakening of the gap filaments in myofibrils. Meat Sci. 10: 207-233
46. Lusby, M., J. F. Ridpath, F. C. Parrish, Jr., and R. M. Robson. 1983. Effect of postmortem storage on degradation of the myofibrillar protein titin in bovine longissimus muscle. J. Food Sci. 48: 1787-1790, 1795.
47. MacDougall, D. R. 1983. Instrumental assessment of the appearance of foods. In Sensory quality in foods and beverage, eds. A. A. Williams and R. K. Atkin, 121-129. Chicester, UK: Ellis Horwood.
48. Macfarlane, J. J. 1973. Pre-rigor pressurization of muscle: Effects on pH, shear value and taste panel assessment. J. Food Sci. 38: 294-298
49. Macfarlane, J. J. 1985. High pressure technology and meat quality. In Developments in meat science 3, ed. R. A. Lawrie, 155-184. London: Elsevier Applied Science.
50. Macfarlane, J. J., J. J. Mckenzie, R. H. Turner, and P. N. Jones. 1981. Pressure treatment of meat: Effect on thermal transitions and shear values. Meat Sci. 5: 307-317
51. Macfarlane, J. J., and D. J. Morton. 1978. Effects of pressure treatment on the ultrastructure of striated muscle. Meat Sci. 2: 281-288
52. Martino, M. N., L. Otero, P. D. Sanz, and N. E. Zaritzky. 1998. Size and location of ice crystals in pork frozen by high-pressure-assisted freezing as compared to classical methods. Meat Sci. 50: 303-313
53. Maruyama, K., S. Kimura, H. Yoshidomi, H. Sawada, and M, Kikuchi. 1984. Molecular size and shape of β-connectin, an elastic protein of striated muscle. J. Biochem. 95: 1423-1433
54. Maruyama, K., T. Yoshioka, H. Higuchi, K. Ohashi, S. Kimura, and R. Natori. 1985. Connectin filaments link thick fi1aments and Z-lines in frog skeletal muscle as revealed by immunoelectron microscopy. J. Cell Biol. 101: 2167-2172
55. Massaux, C., F. Bera, B. Steyer, M. Cindic, and C. Deroanne. 1999a. High hydrostatic pressure effects on freezing and thawing of pork meat: Quality preservation, processing times and high pressure treatment advantages. In Advances in pressure bioscience and biotechnology, ed. H. Ludwig, 485-488. Heidelberg, Germany: Springer.
56. Massaux, C., F. Bera, B. Steyer, M. Cindic, and C. Deroanne. 1999b. High hydrostatic pressure effects on freezing and thawing processes of pork meat. In Advances in pressure bioscience and biotechnology, ed. H. Ludwig, 497-500. Heidelberg, Germany: Springer.
57. Minerich, P. L., and R. Krug. 2003. Case study in real world: Use of high pressure technology for processing hams. In 2003 IFT annual meeting technical program, 89. Chicago: IFT.
58. Nishimura, T., A. Hattori, and K. Takahashi. 1995. Structural weakening of intramuscular connective tissue during conditioning of beef. Meat Sci. 39: 127-133
59. 2+- enhanced ATPase activity of rabbit myofibrils. Meat Sci. 43: 145-155
60. Nose, M., M. Yamagishi, and M. Hattori. 1992. Development of a processing system of meat and meat products by introducing high pressure treatment. In High pressure and biotechnology, eds. C. Balny, R. Hayashi, K. Heremans, and P. Masson, 321-323. Montrouge: John Libbey Eurotext.
61. O’Shea, J. M., D. J. Horgan, and J. J. Macfarlane. 1976. Some effects of pressure treatment on actomyosin systems. Aust. J. Biol. Sci. 29: 197-207
62. Ohmori, T., T. Shigehisa, S. Taji, and R. Hayashi. 1992. Biochemical effects of high hydrostatic pressure on the lysosomal enzymes and proteases. Agric. Biol. Chem. 56: 1285-1288
63. Okamoto, A., and A. Suzuki. 2002. Effects of high hydrostatic-thawing on pork meat. In Trends in high pressure bioscience and technology, ed. R. Hayashi, 571-576. Amsterdam: Elsevier Science.
64. Olson, D. G., F. C. Parrish, Jr., and M. H. Stromer. 1977. Myofibrillar fragmentation and shear resistance of three bovine muscles during postmortem storage. J. Food Sci. 41: 1036-1041
65. Ooi, T. 1994. Effects of pressure on thermal denaturation of proteins. In High pressure bioscience (in Japanese), eds. R. Hayashi, S. Kunugi, S. Shimada, and A. Suzuki, 16-24. Kyoto, Japan: Sanei Shuppan.
66. Orlien, V., and E. Hansen. 2000. Lipid oxidation in high pressure processed chicken breast muscle during chill storage: Critical working pressure in relation to antioxidation mechanism. Eur. Food Res. Technol. 211: 99-104
67. 2+-enhanced ATPase activity as an index of myofibrillar ageing in beef. Meat Sci. 11: 79-88
68. Patterson, B. C., and F. C. Parrish, Jr. 1986. A sensory panel and chemical analyses of certain beef chuck muscles. J. Food Sci. 51: 876-879, 896.
69. Patterson, M. F., M. Quinn, R. Simpson, and A. Gilmour. 1996. High pressure inactivation in foods of animal origin. In High pressure bioscience and biotechnology, eds. R. Hayashi and C. Balny, 267-272. Amsterdam: Elsevier Science.
70. Ratcliff, D., P. E. Bouton, A. L. Ford, P. V. Harris, J. J. Macfarlane, and J. M. O’Shea. 1977. Pressure-heat treatment of post-rigor muscle: Objective-subjective measurements. J. Food Sci. 42: 857-859, 865.
71. Riffero, L. M., and Z. A. Holmes. 1983. Characteristics of pre-rigor pressurized versus conventionally processed beef cooked by microwave and by boiling. J. Food Sci. 48: 346-350, 372.
72. Saccani, G., G. Parolari, E. Tanzi, and S. Rabbuti. 2004. Sensory and microbiological properties of dried hams treated with high hydrostatic pressure. In Proceedings of 50th International Congress of Meat Science and Technology, 726-729. Helsinki, Finland: University of Helsinki.
73. Sano, T., S. F. Noguchi, J. J. Matsumoto, and T. Tsuchiya. 1988. Dynamic viscoelastic behaviour of natural actomyosin and myosin during thermal gelation. J. Food Sci. 53: 924-928
74. Seki, N., and T. Watanabe. 1984. Connectin content and its postmortem changes in fish muscle. J. Biochem. 95: 1161-1167
75. Shoji, T., H. Saeki, M. Wakameda, and M. Nonaka. 1990. Gelation of salted paste of Alaska pollack by high hydrostatic pressure and changes in myofibrillar protein in it. Bull. Jap. Soc. Sci. Fish. 56: 2069-2076
76. Suzuki, A. 2002. High pressure-processed foods in Japan and the world. In Trends in high pressure bioscience and technology, ed. A. Hayashi, 365-374. Amsterdam: Elsevier Science.
77. Suzuki, A., N. Homma, A. Fukuda, K. Hirao, T. Uryu, and Y. Ikeuchi. 1994. Effects of high pressure treatment on the flavour-related components in meat. Meat Sci. 37: 369-379
78. Suzuki, A., K. Hoshino, E. Sasaki, N. Sano, M. Nakane, Y. Ikeuchi, and M. Saito. 1987. Postmortem changes in native connectin in rabbit skeletal muscle. Agric. Biol. Chem. 52: 1439-1444
79. Suzuki, A., K. Kim, N. Honma, Y. Ikeuchi, and M. Saito. 1992. Acceleration of meat conditioning by high pressure. In High pressure and biotechnology, eds. C. Balny, R. Hayashi, K. Heremans and P. Masson, 219-227. Montrouge: John Libbey Eurotext.
80. Suzuki, A., K. Kim, and Y. Ikeuchi. 1996. Proteolytic cleavage of connectin/titin. Adv. Biophys. 33: 53-64
81. Suzuki, A., K. Kim, H. Tanji, and Y. Ikeuchi. 1992. Effects of high hydrostatic pressure on postmortem muscle. Recent Res. Devel. in Agri. Biol. Chem. 2: 307-331
82. 2+ release from rabbit sarcoplasmic reticulum. Biosci. Biotech. Biochem. 57: 862-863
83. Suzuki, A., A. Okamoto, Y. Ikeuchi, and M. Saito. 1994. Effect of high pressure treatment on sarcoplasmic reticulum. High Pressure Res. 12: 255-261
84. Suzuki, A., M. Watanabe, Y. Ikeuchi, M. Saito, and K. Takahashi. 1993. Effects of high pressure treatment on the ultrastructure and thermal behaviour of beef intramuscular collagen. Meat Sci. 35: 17-25
85. Suzuki, A., M. Watanabe, K. Iwamura, Y. Ikeuchi, and M. Saito. 1990. Effect of high pressure treatment on the ultrastructure and myofibrillar protein of beef skeletal muscle. Agric. Biol. Chem. 54: 3085-3091
86. Suzuki, T. 1991. Effect of pressure treatment on the muscle structure and heat-induced gelation of myofibril proteins. In High pressure science for food, ed. R. Hayashi, 273-284. Kyoto, Japan: Sannei Shuppan.
87. Takahashi, K., T. Fukazawa, and T. Yasui. 1967. Formation of myofibrillar fragments and reversible contraction of sarcomere in chicken pectoral muscle. J. Food Sci. 32: 409-413
88. Takahashi, K., and H. Saito. 1979. Post-mortem changes in skeletal muscle connectin. J. Biochem. 85: 1539-1542
89. Tatsumi, R., A. Hattori, and K. Takahashi. 1996. Splitting of connectin/titin filaments into β- connectin/T2 and a 1,200-kDa subfragment by 0.1mM calcium ions. Adv. Biophys. 33: 65-77
90. Ueno, Y., Y. Ikeuchi, and A. Suzuki. 1999. Effect of high pressure treatment on intramuscular connective tissue. Meat Sci. 52: 143-150
91. Wang, K., J. McClure, and A. Tu. 1979. Titin: Major myofibrillar component. Proc. Natl. Acad. Sci, USA. 76: 3698-3702
92. Yamamoto, K., T. Miura, and T. Yasui. 1990. Gelation of myosin filament under high hydrostatic pressure. Food Struct. 9: 269-277
93. Yasui, T., M. Ishioroshi, and K. Samejima. 1980. Heat-induced gelation in the presence of actin. J. Food Biochem. 4: 61-78
94. Yuste, J., M. Cappellas, R. Pla, D. Y. C. Fung, and M. Mor-Mur. 2001. High pressure processing for food safety and preservation: A review. J. Rapid Meth. and Autom. in Microbiol. 9: 1-10
95. Zhao, Y., R. A. Flores, and D. G. Olson. 1998. High hydrostatic pressure effects on rapid thawing of frozen beef. J. Food Sci. 63: 272-275
96. Zipp, A., and W. Kauzmann. 1973. Pressure denaturation of metmyoglobin. Biochem. 12: 4217-4428