Denaturation of tilapia myosin fragments by high hydrostatic pressure

Journal of Food Science

Volumn 69, Issue 8, 2004, Pages

  Ko, W C ^a   Hwang, J S ^b   Jao, C L ^c   Hsu, K C ^d  

^a DA YEH UNIVERSITY   (Taiwan)

^b HUNGKUANG UNIVERSITY   (Taiwan)

^c TUNG FANG INSTITUTE OF TECHNOLOGY   (Taiwan)

^d CHUNG SHAN MEDICAL UNIVERSITY   (Taiwan)

Author keywords

Denaturation; Hydrostatic pressure; Rod; S 1

Indexed keywords

TILAPIA;

EID: 7444253960     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2621.2004.tb09907.x     Document Type: Article

References (18)

1. Davis JS. 1981. The influence of pressure on the self-assembly of the thick filament from the myosin of vertebrate skeletal muscle. Biochem. J. 197(2):301-8.
2. Deng J, Toledo RT, Lillard DA. 1976. Effect of temperature and pH on protein-protein interaction in actomyosin solutions. J. Food Sci. 41(2):273-7.
3. Dickinson E, Pawlowsky K. 1996. Effect of high-pressure treatment of protein on the rheology of flocculated emulsions containing protein and polysaccharide. J Agric Food Chem 44:2992-3000.
4. Gill TA, Conway JT. 1989. Thermal aggregation of cod muscle proteins using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide as a zero-length cross-linker. Agric Biol Chem 53:2553-62.
5. Hsu KC, Ko WC 2001. Effect of hydrostatic pressure on aggregation and viscoelastic properties of tilapia (Orechromis niloticus) myosin. J Food Sci 66(8):1158-62.
6. Ikeuchi Y, Tanji H, Kim K, Suzuki A. 1992. Mechanism of heat-induced gelation of pressurized actomyosin: pressure-induced changes in actin and myosin in actomyosin. J Agric Food Chem 40:1756-61.
7. Ishizaki S, Tanaka M, Takai R, Taguchi T. 1995. Stability of fish myosins and their fragments to high hydrostatic pressure. Fisheries Sci 61(6):989-92.
8. Ko WC, Jao CL, Hsu KC. 2003. Effect of hydrostatic pressure on molecular conformation of tilapia (Orechromis niloticus) myosin. J Food Sci 68(4):1192-5.
9. Samejima K. 1978. The studies of the denaturation and the heat gelling properties of myosin and its helical subfragments. J Coll Dairy 7(1):143-250.
10. Samejima K, Hara S, Yamamoto K, Asghar A, Yasui T. 1985. Physicochemical properties and heat-induced gelling of cardiac myosin in model system. Agric Biol Chem 49(10):2975-83.
11. 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(6):1412-8.
12. Sano T, Noguchi SF, Matsumoto JJ, Tsuchiya T. 1990. Thermal gelation characteristics of myosin subfragments. J Food Sci 55(1):55-8, 70.
13. Sano T, Noguchi SF, Tsuchiya T, Matsumoto II. 1988. Dynamic viscoelastic behavior of natural actomyosin and myosin during thermal gelation. J Food Sci 53(3):924-8.
14. Sano T, Ohno T, Otsuka-Fuchino H, Matsumoto II, Tsuchiya T. 1994. Carp natural actomyosin: thermal denaturation mechanism. J Food Sci 59(5):1002-8.
15. Smyth AB, Smith DM, Vega-Warner V, O'Neill E. 1996. Thermal denaturation and aggregation of chicken breast muscle myosin and subfragments. J Agric Food Chem 44(4):1005-10.
16. Taguchi T, Ishizaka H, Tanaka M, Nagashima Y, Amano K. 1987. Protein-protein interaction of fish myosin fragments. J Food Sci 52(4):1103-4.
17. Takahashi K. 1978. Topography of the myosin molecule as visualized by an improved negative staining method. J Biochem 83(5):905-9.
18. Yamamoto K, Hayashi S, Yasui T. 1993. Hydrostatic pressure-induced aggregation of myosin molecules in 0.5 M KCl at pH 6.0. Biosci Biotech Biochem 57(3):383-9.