The unexpected behaviour of 1,5-glucono-δ-lactone-induced myosin gels upon dialysis

Food Chemistry

Volumn 55, Issue 3, 1996, Pages 271-279

  Ngapo, T M ^a   Wilkinson, B H P ^a   Chong, R ^a  

^a MASSEY UNIVERSITY   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

LACTONE DERIVATIVE; MUSCLE PROTEIN; MYOSIN;

ANIMAL TISSUE; ARTICLE; CHEMISTRY; DIALYSIS; GEL; NONHUMAN;

ANIMALIA;

EID: 0029932351     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/0308-8146(95)00131-X     Document Type: Article

References (16)

1. AOAC (1990). Official Methods of Analysis of the Association of Official Analytical Chemists (15th edn), ed. K. Helrich. Association of Official Analytical Chemists Inc., Virginia.
2. Arteaga, G. E. & Nakai, S. (1992). Thermal denaturation of turkey breast myosin under different conditions: effect of temperature and pH, and reversibility of the denaturation. Meat Sci., 31, 191-200.
3. Dudziak, J. A. & Foegeding, E. A. (1988). Isolation of actomyosin and myosin from post-rigor turkey breast and thigh. J. Food Sci., 53, 1287-9, 1339.
4. Egelandsdal, B., Fretheim, K. & Harbitz, O. (1986). Dynamic rheological measurements on heat-induced myosin gels: an evaluation of the methods suitability for the filamentous gels. J. Sci. Food Agric., 37, 944-54.
5. Ferry, J. D. (1948). Protein gels. Adv. Protein Chem., 4, 1-78.
6. Foegeding, E. A., Allen, C. E. & Dayton, W. R. (1986). Effect of heating rate on thermally formed myosin, fibrinogen and albumin gels. J. Food Sci., 51, 104-8, 112.
7. Gornall, A. G., Bardawill, C. J. & David, M. M. (1949). Determination of serum proteins by means of the biuret reaction. J. Biol. Chem., 177, 751-66.
8. Hermansson, A.-M. (1979). Aggregation and denaturation involved in gel formation. In Functionality and Protein Structure. A.C.S. Symposium Series 92, ed. A. Pour-El. American Chemistry Society, Washington DC.
9. Locker, R. H. & Wild, D. J. C. (1984). The fate of the large proteins of the myofibril during tenderising treatments. Meat Sci., 11, 89-108.
10. Rogers, E. M., Karr, T., Biedermann, K., Vero, H. & Harrington, F. W. (1987). Thermal stability of myosin rod from various species. Biochemistry, 26, 8703-8.
11. Samejima, K., Takahashi, K. & Yasui, T. (1976). Heatinduced denaturation of myosin total rod. Agric. Biol. Chem., 40, 2455-64.
12. Samejima, K., Ishioroshi, M. & Yasui, T. (1981). Relative roles of the head and tail portions of the molecule in heat induced gelation of myosin. J. Food Sci., 46, 1412-18.
13. Szent-Györgyi, A. (1951). Chemistry of Muscular Contraction (2nd edn). Academic Press, Inc., New York [via Fretheim, K., Egelandsdal, B., Harbitz, O. & Samejima, K. (1985). Slow lowering of pH induces gel formation of myosin. Food Chem., 18, 169-78.]
14. Szent-Györgyi, A. (1951). Chemistry of Muscular Contraction (2nd edn). Academic Press, Inc., New York [via Fretheim, K., Egelandsdal, B., Harbitz, O. & Samejima, K. (1985). Slow lowering of pH induces gel formation of myosin. Food Chem., 18, 169-78.]
15. Venable, J. M. & Coggleshall, R. (1965). A simplified lead citrate stain for use in electron microscopy. J. Cell Biol., 25, 407-8.
16. Wright, D. J. & Wilding, P. (1984). Differential scanning calorimetric study of muscle and its proteins: myosin and its subfragments. J. Sci. Food Agric., 35, 357-72.