Physicochemical changes and mechanism of heat-induced gelation of arrowtooth flounder myosin

Journal of Agricultural and Food Chemistry

Volumn 48, Issue 4, 2000, Pages 1016-1023

  Visessanguan, Wonnop ^a   Ogawa, Masahiro ^b   Nakai, Shuryo ^b   An, Haejung ^a  

^a OREGON STATE UNIVERSITY   (United States)

^b UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

Arrowtooth flounder; Denaturation; Gelation; Myosin; Surimi

Indexed keywords

MYOSIN;

ANIMAL; ARTICLE; CHEMISTRY; DIFFERENTIAL SCANNING CALORIMETRY; FISH; FLOUNDER; GEL; HEAT; HEATING; HYDROPHOBICITY; IONIC STRENGTH; NONHUMAN; OSMOLARITY; PHYSICAL CHEMISTRY; PROTEIN MODIFICATION; SKELETAL MUSCLE; THERMODYNAMICS;

ANIMALS; CALORIMETRY, DIFFERENTIAL SCANNING; FLOUNDER; GELS; HEAT; MUSCLE, SKELETAL; MYOSINS; OSMOLAR CONCENTRATION; THERMODYNAMICS;

EID: 0034055958     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf9900332     Document Type: Article

References (53)

1. Chan, J. K.; Gill, T. A. Thermal aggregation of mixed fish myosins. J. Agric. Food Chem. 1994, 42, 2649-2655.
2. Chan, J. K.; Gill, T. A.; Paulson, A. T. The dynamics of thermal denaturation of fish myosins. Food Res. Int. 1992, 25, 117-123.
3. Chan, J. K.; Gill, T. A.; Paulson, A. T. Thermal aggregation of myosin subfragments from cod and herring. J. Food Sci. 1993, 58, 1057-1069.
4. Davies, J. R.; Ledward, D. A.; Bardsley, R. G.; Poulter, R. G. Species dependence of fishmyosin stability to heat and frozen storage. Int. J. Food Sci. Technol. 1994, 29, 287-301.
5. Egelandsdal, B.; Martinsen, B.; Autio, K. Rheological parameters as predictor of protein functionality - A model study using myofibrils of different fiber-type composition. Meat Sci. 1995, 39, 97-111.
6. Ellman, G. L. Tissue sulfhydryl groups. Arch. Biochem. Biophys. 1959, 82, 70-77.
7. Gill, T. A.; Conway, J. T. Thermal aggregation of cod muscle proteins using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide as a zero length cross-linker. Agric. Biol. Chem. 1989, 53, 2553.
8. Gill, T. A.; Chan, J. K.; Phonchareon, K. F.; Paulson, A. T. Effect of salt concentration and temperature on heat-induced aggregation and gelation of fish myosin. Food Res. Int. 1992, 25, 333.
9. Goodno, C. C.; Harris, T. A.; Swenson, C. A. Thermal transitions of myosin and its helical fragments. Regions of structural instability in the myosin molecule. Biochemistry 1976, 15, 5157.
10. Greene, D. H.; Babbitt, J. K. Control of muscle softening and protease-parasite interactions in Aroowtooth flounder, Ateresthes stomias. J. Food Sci. 1990, 55, 579-580.
11. Hamada, M. Mechanical behavior and cross linkages of heat-induced myosin gel. Nippon Suisan Gakkaishi 1992, 58, 89-93.
12. Hamai, M.; Konno, K. Thermal stability as a probe of S-1 structure. J. Biochem. 1989, 106, 803-807.
13. Hayakawa, S.; Nakai, S. Contribution of hydrophobicity, net charge and sulfhydryl groups to thermal properties of ovalbumin. Can. Inst. Food Sci. Technol. J. 1985, 18, 290-295.
14. Holzwarth, G.; Doty, P. The ultraviolet circular dichroism of polypeptides. J. Am. Chem. Soc. 1965, 87, 218-228.
15. Ishioroshi, M.; Samejima, K.; Yasui, T. Heat-induced gelation of myosin: Factors of pH and salt concentrations. J. Food Sci. 1979, 44, 1280-1283.
16. Johnston, I. A.; Frearson, N.; Goldspink, G. The effects of environmental temperature on the properties of myofibrillar adenosine triphosphatase from various species of fish. Biochem. J. 1973, 133, 735-738.
17. Li-Chan, E.; Nakai, S.; Wood, D. Relationship between functional (fat-binding, emulsifying) and physicochemical properties of muscle proteins. Effects of heating, freezing, pH and species. J. Food Sci. 1985, 50, 1034.
18. Lin, T. M.; Park, J. W. Solubility of salmon myosin as affected by conformational changes at various ionic strengths and pH. J. Food Sci. 1998, 63, 215-218.
19. Lopez-Lacomba, J. L.; Guzman, M.; Cortijo, M.; Mateo, P. L.; Aguirre, R.; Harvey, S. C.; Cheung, H. C. Differential scanning calorimetric study of the thermal unfolding of myosin rod, light meromysin, and sub-fragment 2. Biopolymers 1989, 28, 2143-2159.
20. Lowey, S.; Slayter, H. S.; Weeds, A. G.; Baker, H. Substructure of the myosin molecule. I. Subfragments of myosin by enzymatic degradation. J. Mol. Biol. 1969, 42, 1.
21. Lowry, Q. H.; Rosebrough, N. J.; Farr, L. A.; Randall, R. J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 1951, 193, 265.
22. Maita, T.; Yajima, E.; Nagata, S.; Miyanishi, T.; Nakayama, S.; Matsuda, G. The primary structure of skeletal muscle myosin heavy chain: IV. Sequence of the rod, and the complete 1,938-residue sequence of the heavy chain. J. Biochem. 1991, 75-87.
23. Martone, C. B.; Busconi, L.; Folco, E. J.; Trucco, R. E.; Sanchez, J. J. A simplified myosin preparation from Marine fish species. J. Food Sci. 1986, 51, 1554-1555.
24. McCubbin, D. W.; Kay, M. C. In Methods in Enzymology; Frederiksen, D. W., Cunningham, L. W., Eds.; Academic Press: New York, 1982;Vol. 85, p 629.
25. Monta, J. I.; Choe, I. S.; Yamamoto, K.; Samejima, K.; Yasui, T. Heat-induced gelation of myosin from leg and breast muscles of chicken. Agric. Biol. Chem. 1987, 11, 2895-2900.
26. Niwa, E. Chemistry of surimi gelation. In Surimi Technology; Lanier, T. C., Lee, C. M., Eds.; Dekker: New York, 1992; p 389.
27. Niwa, E.; Matsuura, Y.; Nowsad, A. A. K.; Kanoh, S. Species-specificity of suwari gel-formability of flesh fish paste in which transglutaminase was inactivated. Fish. Sci. 1995, 61, 107-109.
28. Ogawa, M.; Ehara, T.; Tamiya, T.; Tsuchiya, T. Thermal stability of fish myosin. Comp. Biochem. Physiol. 1993, 106B, 517-521.
29. Park, J. W.; Lanier, T. C. Effects of salt and sucrose addition on thermal denaturation and aggregation of water-leached fish muscle. J. Food Biochem. 1990, 14, 395.
30. Park, J. W.; Lin, T. M.; Yonngsawatdigul, J. New developments in manufacturing of surimi and surimi seafood. Food Rev. Int. 1997, 577-610.
31. Parsons, N.; Knight, P. Origin of variable extraction of myosin from myofibrils treated with salt and pyrophosphate. J. Sci. Food Agric. 1990, 51, 71.
32. Pearson, A. M.; Young, R. B. Proteins of the thick filaments. In Muscle and Meat Biochemistry; Pearson, A. M., Young, R. B., Eds.; Academic Press: New York, 1989; p 74.
33. Privalov, P. L Stability of proteins: proteins which do not present a single cooperative system. Adv. Protein Chem. 1982, 35, 85.
34. Rattrie, N. W.; Regenstein, J. M. Action of crude papain on actin and myosin heavy chains isolated from chicken breast muscle. J. Food Sci. 1977, 42, 1159-1163.
35. Riddles, P. W.; Blakeley, R. L.; Zerner, B. Methods Enzymol. 1983, 91, 49-61.
36. Roussel, H.; Cheftel, J. C. Mechanisms of gelation of sardine proteins-Influence of thermal processing and of various additives and texture and protein solubility of kamaboko gels. Int. J. Food Sci. Technol. 1990, 25, 260-280.
37. Samejima, K.; Ishiroshi, M.; Yasui, T. Relative roles of the head and tail portions of the molecule in heat induced gelation of myosin. J. Food Sci. 1981, 46, 1412-1418.
38. Samejima, K.; Yamauchi, H.; Asghar, A.; Yasui, T. Role of myosin heavy chains from rabbit skeletal muscle in the heat-induced gelation mechanism. Agric. Biol. Chem. 1984, 48, 2225.
39. Sano, T.; Noguchi, S. F.; Tsuchiya, T. J.; Matsumoto, J. J. Dynamic viscoelastic behaviour of natural actomyosin and myosin during thermal gelation. J. Food Sci. 1988, 53, 924-928.
40. Sano, T.; Noguchi, S. F.; Matsumoto, J. J.; Tsuchiya, T. J. Thermal gelation characteristics of myosin subfragments. J. Food Sci. 1990a, 55, 55.
41. Sano, T.; Noguchi, S. F.; Matsumoto, J. J.; Tsuchiya, T. J. Effect of ionic strength on dynamic viscoelastic behaviour of myosin during thermal gelation. J. Food Sci. 1990b, 55, 51.
42. Sharp, A.; Offer, G. The mechanism of formation of gels from myosin molecules. J. Sci. Food Agric. 1992, 58, 63-73.
43. Smyth, A. B.; Smith, D. M.; O'Neill, E. Disulfide bonds influence the heat-induced gel properties of chicken breast muscle myosin. J. Food Sci. 1998, 63, 584-588.
44. Stones, A. P.; Stanley, D. W. Mechanisms of fish muscle gelation. Food Res. Int. 1992, 25, 381-388.
45. Suzuki, T. Frozen minced meat (surimi). In Fish and Krill Protein Technology: Processing Technology; Applied Science Publishers: London, U.K., 1981; Chapter 3, p 115.
46. Taguchi, T.; Ishizaka, M.; Tanaka, M.; Nagashima, Y.; Amano, K. Protein-protein interaction of fish myosin fragments. J. Food Sci. 1987, 52, 1103.
47. Tsuchiya, T.; Matsumoto, J. T. Isolation, purification, and structure of carp myosin, HMM, and LMM. Nippon Suisan Gakkaishi 1975, 41, 1319-1326.
48. Wang, S. F.; Smith, D. M. Heat-induced denaturation and rheological properties of chicken breast myosin and F-actin in the presence and absence of pyrophosphate. J. Agric. Food Chem. 1994, 42, 2665-2670.
49. Wasson, D. H.; Babbitt, J. K.; French, J. S. Characterization of a heat stable proteasefrom arrowtooth flounder; Atheresthes stomias. J. Aquat. Food Prod. Technol. 1992, 1 (3/4), 167-182.
50. Wicker, L.; Lanier, T. C.; Hamann, D. D.; Akahane, T. Thermal transitions in myosin-ANS fluorescence and gel rigidity. J. Food Sci. 1986, 51, 1540-1543.
51. Xiong, Y. L. A comparison of the rheological characteristics of different fractions of chicken myofibrillar proteins. J. Food Biochem. 1993, 217-227.
52. Xiong, Y. L. Structure-function relationships of muscle proteins. In Food Proteins and Their Applications; Damodaran, S., Paref, A., Eds.; Dekker: New York, 1997; pp 341-392.
53. Yasui, T.; Ishioroshi, M.; Samejima, K. Heat-induced gelation of myosin in the presence of actin. J. Food Biochem. 1980, 4, 61.