Effect of zinc salts on the structure-function of actomyosin from pelagic fish

Process Biochemistry

Volumn 44, Issue 7, 2009, Pages 704-709

  Mathew, Sijo ^a   Shamasundar, B A ^b   Ramesh Kumar, Parigi ^a   Prakash, V ^a  

^a CENTRAL FOOD TECHNOLOGICAL RESEARCH INSTITUTE   (India)

^b University   (India)

Author keywords

ATPase; Far UV circular dichroic spectra; Fish actomyosin; Fluorescence spectra; Oil sardine; Solubility; Zinc chloride; Zinc sulfate

Indexed keywords

ATPASE; FAR UV-CIRCULAR DICHROIC SPECTRA; FLUORESCENCE SPECTRA; OIL SARDINE; ZINC CHLORIDE; ZINC SULFATE;

CHLORINE COMPOUNDS; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYMES; FISH; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; LIGHT POLARIZATION; MEATS; PH EFFECTS; SOLUBILITY; TERNARY SYSTEMS; ZINC;

SALTS;

SARDINELLA LONGICEPS;

EID: 67349083584     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2009.02.018     Document Type: Article

References (30)

1. Rayment I. The structural basis of the myosin ATPase activity. J Biol Chem 271 (1996) 15850-15853
2. Nayak R., Kenney P.B., Slider S., Head M.K., and Killefer J. Myofibrillar protein solubility of model beef batters as affected by low levels of calcium, magnesium and zinc chloride. J Food Sci 63 (1998) 951-954
3. Nayak R., Kenney P.B., Slider S., Head M.K., and Killefer J. Cook yield, texture and gel ultrastrucuture of model beef batters as affected by low levels of calcium, magnesium and zinc chloride. J Food Sci 63 (1998) 945-950
4. Bougatef A., Souissi N., Fakhfakh N., Ellozu-Trki Y., and Nasri M. Purification and characterization of trypsin from viscera of sardine (Sadina pilchardus). Food Chem 102 (2007) 343-350
5. Bezerra R.S., Lin E.J.F., Alencar R.B., Paiva P.M.G., Chaves M.E.C., Coelho L.C.B.B., et al. Process Biochem 40 (2005) 1829-1834
6. Mathew S., and Prakash V. Effect of calcium salts on the properties of proteins from Oil sardine (Sardinella lingiceps) during frozen storage. J Food Sci 71 4 (2006) E178-E183
7. Kim S., and Mendis E. Bioactive compounds from amrine processing byproducts-a review. Food Res Int 39 (2005) 383-393
8. MacDonald G.A., Lanier T.C., and Giesbrecht F. Interaction of sucrose and zinc for cryoprotection of surimi. J Agric Food Chem 44 (1996) 113-118
9. Carpenter J.F., Hand S.C., Crowe L.M., and Crowe J.H. Cryoprotection of phosphofructokinase with organic solutes; characterization of enhanced protection in the presence of divalent cations. Arch Biochem Biophys 250 (1986) 505-512
10. Carpenter J.F., Crowe L.M., and Crowe J.H. Stabilization of phosphofructokinase with sugars during freeze-drying; characterization of enhanced protection in the presence of divalent cation. Biochim Biophys Acta 23 (1987) 109-115
11. Hazen K.C., Bourgeois L.D., and Carpenter J.F. Cryoprotection of antibody by organic solutes and organic solute/divalent cation mixtures. Arch Biochem Biophys 267 (1988) 363-371
12. Berg J.M., and Shi Y. The galvanization of biology: a growing appreciation for the roles of zinc. Science 271 (1996) 1081-1085
13. Berg J.M., and Merkle D.L. On metal ion specificity of zinc finger proteins. J Am Chem Soc 111 (1989) 3759-3761
14. Margassian S.S., and Lowey S. Preparation of myosin and its subfragments from rabbit skeletal muscle. Methods Enzymol 85 (1982) 55-71
15. Mathew S., and Prakash V. Polyhydric alcohols mediated inhibition of calcium activated adenosine triphosphatase activity of fish skeletal muscle actomyosin. Int J Food Prop 8 (2005) 255-265
16. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
17. Perry S.V. Myosine adenosine triphosphatase. Methods Enzymol 2 (1955) 582-588
18. Taussky H.H., and Shorr E. A microcalorimetric method for determination of inorganic phosphorous. J Biol Chem 202 (1953) 675-685
19. Yang J.T., Wu C.C., and Martinez H.M. Calculation of protein conformation from circular dichroism. Methods Enzymol 130 (1986) 208-269
20. Beveridge T., Toma S.J., and Nakai S. Determination of SH and SS groups in some food proteins using Ellman's reagent. J Food Sci 39 (1974) 49-51
21. Karthikeyan M., Shamasundar B.A., Mathew S., Ramesh Kumar P., and Prakash V. Physico-chemical and functional properties of proteins from pelagic fatty fish (Sardinella longiceps) as a function of water washing. Int J Food Prop 7 (2004) 353-365
22. Mathew S., and Prakash V. Changes in strucutural and functional attributes of fish mince proteins in presence of cosolvent during frozen storage. Int J Food Prop 10 (2007) 47-59
23. Park J.W. Ingredient technology and formulation development. Surimi and surimi seafood (2000), Marcel and Dekker Inc., New York p. 343-391
24. Maret W. Zinc coordination environments in proteins determine zinc functions. J Trace Elements Med Biol 19 (2005) 7-12
25. Chan J.K., Gill T.A., and Paulson A.T. The dynamics of thermal denaturation of fish myosins. Food Res Int 25 (1992) 117-123
26. Rayment I., Holden H.M., Whittaker M., Yohn C.B., Lorenz M., Holmes K.C., et al. Structure of the actin-myosin complex and its implications for muscle contraction. Science 261 (1993) 58-65
27. Engelhardt V.A. Adenosinetriphosphatase properties of myosin. Adv Enzymol Relat Subj Biochem 6 (1946) 147-191
28. Wang B., Xiong Y.L., and Srinivasan S. Chemical stability of antioxidant washed beef heart surimi during frozen storage. J Food Sci 2 (1997) 946-948
29. Kato S., and Konno K. Isolation of carp myosin rod and its structural stability. Nippon Suisan Gakkaishi 59 (1993) 539-544
30. Chan J.K., Gill T.A., Thompson J.W., and Singer D.S. Herring surimi during low temperature setting, physicochemical and textural properties. J Food Sci 60 (1995) 1248-1253