Thermal denaturation and aggregation of threadfin bream actomyosin

Food Chemistry

Volumn 83, Issue 3, 2003, Pages 409-416

  Yongsawatdigul, J ^a   Park, J W ^b  

^a SURANAREE UNIVERSITY OF TECHNOLOGY   (Thailand)

^b OREGON STATE UNIVERSITY   (United States)

Author keywords

Actomyosin; Aggregation; Thermal denaturation; Threadfin bream

Indexed keywords

DISULFIDE; FISH PROTEIN; MYOSIN ADENOSINE TRIPHOSPHATASE; THIOL DERIVATIVE;

ALPHA HELIX; ARTICLE; CONFORMATIONAL TRANSITION; ENZYME DENATURATION; ENZYME STRUCTURE; FOOD ANALYSIS; HEATING; HYDROPHOBICITY; PROTEIN AGGREGATION; SURFACE PROPERTY; TEMPERATURE; TEMPERATURE DEPENDENCE; THERMAL ANALYSIS;

ALECTIS CILIARIS; HYPEROGLYPHE POROSA; NEMIPTERIDAE; NEMIPTERUS; NEMIPTERUS BIPUNCTATUS;

EID: 0041386023     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0308-8146(03)00105-5     Document Type: Article

References (38)

1. Bea V.E., Wagner J.R., Crupkin M., Anon M. Thermal denaturation of hake (Merluccius hubbsi) myofibrillar proteins. A differential scanning calorimetric and electrophoretic study. Journal of Food Science. 55:1990;683-687,696.
2. Beveridge T., Arntfield S.D., Murray E.D. Protein structure development in relation to denaturation temperatures. Canadian Institute of Food Science and Technology Journal. 18:1985;189-191.
3. Bradford M. A rapid sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Analytical Biochemistry. 72:1976;248-252.
4. Burke M., Himmelfarb S., Harrington W.F. Studies on the "hinge" region of myosin. Biochemistry. 12:1973;701-709.
5. Chan J.K., Gill T.A., Paulson A.T. Cross-linking of myosin heavy chains from cod, herring, and silver hake during thermal setting. Journal of Food Science. 57:1992;906-912.
6. Davies J.R., Bardsley R.G., Ledward D.A., Poulter R.G. Myosin thermal stability in fish muscle. Journal of the Science of Food and Agriculture. 45:1988;61-68.
7. Egelandsdal B., Fretheim K., Samejima K. Dynamic theological measurements on heat induced myosin gels. effect of ionic strength, protein concentration and addition of adenosine triphosphate or pyrophosphate Journal of the Science of Food and Agriculture. 37:1986;915-926.
8. Ellman G.L. Tissue sulfhydryl groups. Archives of Biochemistry and Biophysics. 82:1959;70-77.
9. Esturk, O., Park, J. W., & Kim, B. Y. (2003). Early determination of rheological properties of Pacific whiting proteins using oscillatory dynamic test. International Journal of Food Science and Technology. Submitted.
10. Hastings R., Rodger G.W., Park R., Matthews A.D., Anderson E.M. Differential scanning calorimetry of fish muscle. the effect of processing and species variation Journal of Food Science. 50:1985;1503-1510.
11. Hayakawa S., Nakai S. Relationships of hydrophobicity and net charge to 12 solubility of milk and soy proteins. Journal of Food Science. 50:1985;486-491.
12. Hermansson A.M. Aggregation and denaturation involved in gel formation. Pour-El A. Functionality and protein structure. 1979;American Chemical Society, Washington, DC.
13. Ishioroshi M., Samejima K., Yasui T. Furhter studies on the roles of the head and tail regions of the myosin molecule in heat-induced gelation. Journal of Food Science. 47:1981;114-120,124.
14. Jiang S.T., Hwang D.C., Chen C.S. Effect of storage temperature on the formation of disulfides and denaturation of milkflsh actontyosin (Chanos chanos). Journal of Food Science. 53:1988;1333-1335,1386.
15. Klesk K., Yongsawatdigul J., Park J.W., Viratchakul S., Virulhakul P. Gel forming ability of tropical tilapia surimi as compared with Alaska pollock and Pacific whiting surimi. Journal of Aquatic Food Product Technology. 9:2000;91-104.
16. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 277:1970;680-685.
17. Lo J.R., Mochisuki Y., Nagashima Y., Tanaka M., iso N., Taguchi T. Thermal transitions of myosins/subfragments from black marlin (Makaira mazara) ordinary and dark muslces. Journal of Food Science. 56:1991;954-957.
18. Monahan F.J., German J.B., Kinsella J.E. Effect of pH and temperature on protein unfolding and thiol/difulfide interchange reactions during heat-induced gealtion of whey proteins. Journal of Agricultural and Food Chemistry. 43:1995;46-52.
19. Morita J.I., Yasui T. Involvement of hydrophobic residues in heat-2 induced gelation of myosin tail subgragments front rabbit skeletal muscle. Agricultural and Biological Chemistry. 55:1991;597-599.
20. Ogawa M., Ehara T., Tamiya T., Tsuchiya T. Thermal stability of fish myosin. Comprehensive Biochemistry & Physiology. 106B:1993;517-521.
21. Ogawa M., Kanarnura J., Miyashita H., Tarniya T., Tsuchiya T. Alpha-helical structure of fish actomyosin. changes during setting Journal of Food Science. 60:1995;297-299.
22. Ogawa M., Nakamura S., Horimoto Y., An H., Tsuchiya T., Nakai S. Raman spectroscopic study of changes in fish actomyosin during setting. Journal of Agricultural and Food Chemistry. 47:1999;3309-3318.
23. Park J.W., Yongsawatdigul J., Lin T.M. Rheological behavior and potential cross-linking of Pacific whiting surimi. Journal of Food Science. 59:1994;773-776.
24. Price, N. (1996). Circular dichroism in protein analysis. In Encyclopedia of molecular biology and molecular medicine. Weinheim, New York.
25. Sano T., Noguchi S.F., Matsumoto J.J., Tsuchiya T. Thermal gelation characteristics of myosin subfragrnents. Journal of Food Science. 55:1990;55-58,70.
26. Sano T., Ohno T., Otsuka-Fuchino H., Matsumoto J.J., Tsuchiya T. Carp natural actomyosin. thermal denaturation mechanism Journal of Food Science. 59:1994;1002-1008.
27. Smyth A.B., Smith D.M., Vega-Warner V., O'Neill E. Thermal denaturation and aggregation of chicken breast muscle myosin and subfragments. Journal of Agricultural and Food Chemistry. 44:1996;1005-1010.
28. Togashi M., Kakinuma M., Nakaya M., Ooi T., Watanabe S. Differential scanning calorimetry and circular dichroism spectrometry of walleye Pollack myosin and light meromyosin. Journal of Agricultural and Food Chemistry. 50:2002;4803-4811.
29. Visessanguan W., Ogawa M., Nakai S., An H. Physicochemical changes and mechanism of heat-induced gelation of arrowtooth flounder myosin. Journal of Agricultural and Food Chemistry. 48:2000;1016-1023.
30. Wicker L., Lanier T.C., Harnann D.D., Akahane T. Thermal transition in myosin-ANS fluorescence and gel rigidity. Journal of Food Science. 51:1986;1540-1543,1562.
31. Wright D.J., Leach I.B., Wilding P. Differential scanning calorimetric studies of muscle and its constituent proteins. Journal of the Science of Food and Agriculture. 28:1977;557-564.
32. Wright D.J., Wilding P. Differential scanning calorimetric study of muscle and its proteins. myosin and its subfragments Journal of the Science of Food and Agriculture. 35:1984;357-372.
33. Wu J.Q., Hamann D.D., Foegeding E.A. Myosin gelation kinetic study based in rheological measurements. Journal of Agricultural and Food Chemistry. 39:1991;229-236.
34. Xiong Y.L., Blanchard S.P. Dynamic gelling properties of myofibrillar protein from skeletal muscles of different chicken parts. Journal of Agricultural and Food Chemistry. 42:1994;670-674.
35. Xiong Y.L., Blanchard S.P. Myofibrillar protein gelation: viscoelastic changes related to heating procedures. Journal of Food Science. 59:1994;734-738.
36. Yasui T., Ishioroshi M., Samejima K. Effect of actomyosin on heat induced gelation of myosin. Agricultural and Biological Chemistry. 46:1982;1049-1059.
37. Yongsawatdigul J., Park J.W. Thermal aggregation and dynamic rheological properties of Pacific whiting and cod myosins as affected by heating rate. Journal of Food Science. 64:1999;679-683.
38. Yongsawatdigul J., Park J.W., Worratao A. Effect of endogeous transglutaminase on threadfin bream surimi gelation. Journal of Food Science. 67:2002;3258-3263.