Differences in properties of myofibrillar proteins from bovine semitendinosus muscle after hydrostatic pressure or heat treatment

Journal of the Science of Food and Agriculture

Volumn 87, Issue 1, 2007, Pages 40-46

  Lee, Eun Jung ^a   Kim, Yun Ji ^a   Lee, Nam Hyouck ^a   Hong, Seok In ^a   Yamamoto, Katsuhiro ^b  

^a Korea Food Research Institute   (South Korea)

^b RAKUNO GAKUEN UNIVERSITY   (Japan)

Author keywords

Heat treatment; Hydrostatic pressure; Inactivation rate; Myofibrillar protein; Soluble protein

Indexed keywords

BOS TAURUS;

EID: 33846080109     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.2656     Document Type: Article

References (34)

1. Yamamoto K, Miura T and Yasui T, Gelation of myosin filament under high hydrostatic pressure. Food Struct 9:269-277 (1990).
2. Weber G, Dynamics of oligomeric proteins. J Mol Liq 42:255-268 (1989).
3. Balny C and Masson P, Effects of high pressure on proteins. Food Rev Int 9:611-628 (1993).
4. Gross M and Jaenicke R, Proteins under pressure: the influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes. Eur J Biochem 221:617-630 (1994).
5. Masson P and Clery C, Pressure effects on structure and activity of cholinesterase: in Enzymes of Cholinesterase Family, ed. by Quinn DM. Plenum, New York, NY, pp. 113-121 (1995).
6. Cheftel JC and Culioli J, Effects of high pressure on meat: a review. Meat Sci 46:211-236 (1997).
7. Macfarlane JJ, High pressure technology and meat quality, in Developments in Meat Science - 1, ed. by Lawrie R. Elsevier Applied Science, London, pp. 155-184 (1985).
8. Suzuki T, Uehara T and Kamoi I, Effect of pressure treatment on the heat-induced gelation of actomyosin. Anim Sci Technol (Jpn) 62:154-160 (1991).
9. Suzuki A, Watanabe M, Iwamura K, Ikeuchi Y and Saito M, Effect of high pressure treatment on the ultrastructure and myofibrillar protein of beef skeletal muscle. Agric Biol Chem 54:3085-3091 (1990).
10. Yamamoto K, Yoshida Y, Morita J and Yasui T, Morphological and physicochemical changes in the myosin molecules induced by hydrostatic pressure. J Biochem 116:215-220 (1994).
11. Yamamoto K, Electron microscopy of thermal aggregation of myosin. J Biochem 108:896-898 (1990).
12. Samajima K, Ishioroshi M and Yasui T, Relative roles of the head and tail portions of the molecule in heat-induced gelation of myosin. J Food Sci 46:1412-1418 (1981).
13. Sano T, Noguchi SF, Matsumoto JJ and Tauchiya T, Effect of ionic strength on dynamic viscoelastic behavior of myosin during thermal gelation. J Food Sci 55:51-70 (1990).
14. Whiting RC, Ingredients and processing factors that control muscle protein functionality. Food Technol 42:104-114, 210 (1988).
15. Messens W, Van Camp J and Huyghebaert A, The use of high pressure to modify the functionality of food proteins. Trends Food Sci Technol 8:107-112 (1997).
16. Ishioroshi M, Samejima K and Yasui T, Heat-induced gelation of myosin filaments at a low salt concentration. Agric Biol Chem 47:2809-2816 (1983).
17. Yamamoto K, Hayashi S and Yasui T, Hydrostatic pressure-induced aggregation of myosin molecules in 0.5 M KCl at pH 6.0. Biosci Biotechnol Biochem 57:383-389 (1993).
18. 2+ specific removal of Z lines from rabbit skeletal muscle. J Cell Biol 52:367-381 (1972).
19. Jiang SZ, Hwang DC and Chen CS, Denaturation and change in SH group of actomyosin from milkfish (Chanos chanos) during storage at -20°C. J Agric Food Chem 36:433-437 (1988).
20. Bowker BC, Swartz DR, Grant AL and Gerrard DE, Myosin heavy chain isoform composition influences the susceptibility of actin-activated S1 ATPase and myofibrillar ATPase to pH inactivation. Meat Sci 71:341-350 (2005).
21. Fiske CH and Subbarow Y, The colorimetric determination of phosphorus. J Biol Chem 66:375-400 (1926).
22. Matsumoto I, Ooizumi T and Arai K, Protective effect of sugar on freeze-denaturation of carp myofibrillar protein. Nippon Suisan Gakkaish 51:833-839 (1985).
23. Li-Chan E, Heat-induced changes in the proteins of whey protein concentrate. J Food Sci 48:47-56 (1983).
24. Gornall AG, Bardawill CJ and David MM, Determination of serum proteins by means of the biuret reaction. J Biol Chem 177:751-766 (1949).
25. Laemmli VK, Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685 (1970).
26. Neuhoff V, Arold N, Taube D and Ehrhardt N, Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G250 and R-250. Electrophoresis 9:255-262 (1998).
27. SAS Institute, SAS User's Guide. Statistical Analysis Systems Institute, Cary, NC (1996).
28. 2+-regulation of the actin-activated Mg-ATPase activity of myosin from Physarum polycephalum plasmodia. J Biochem 99:1433-1446 (1986).
29. Makita T, Hane H, Kanyama N and Shimizu K, Behavior of water under high pressure in relation to the food processing, in High Pressure Science for Food, ed. by Hayashi R. San-ei Shuppan, Kyoto, pp. 93-100 (1991).
30. Stabursvik E and Martens H, Thermal denaturation of proteins in post rigor muscle tissue as studied by differential scanning calorimetry. J Sci Food Agric 31:1034-1042 (1980).
31. Yang R, Hong SP, Shin WC and Song JC, Study on the thermostability of contractile myofibrillar proteins from fish species. Kor J Food Sci Technol 20:862-867 (1988).
32. Xiong YL, Brekke CJ and Leung Jr HK, Thermal denaturation of muscle proteins from different species and muscle types as studied by differential scanning calorimetry. Can Inst Food Sci Technol J 2:357-362 (1987).
33. Macfarlane JJ, Pre-rigor pressurization of muscle: effects on pH, shear value and taste panel assessment. J Food Sci 38:294-298 (1973).
34. Ikeuchi Y, Tanji H, Kim K and Suzuki A, Mechanism of heat-induced gelation of pressurized actomyosin: pressure-induced changes in actin and myosin in actomyosin. J Agric Food Chem 40:1756-1761 (1992).