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

Mathew, Sijo and Shamasundar, B. A. and Ramesh Kumar, Parigi and Prakash, V. (2009) Effect of zinc salts on the structure-function of actomyosin from pelagic fish. Process Biochemistry, 44 (7). pp. 704-709. ISSN 1359-5113

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The effect of zinc salts, zinc chloride and zinc sulfate on the structure and ATPase enzyme activity of actomyosin from pelagic fish (Sardinella longiceps) has been investigated. ATPase enzyme activity decreased in the presence of both the zinc salts. The inhibitory effect is present in both pH of 7.0 and 9.0. At concentration of 1נ10-3M of zinc salts, complete inhibition of ATPase enzyme activity is observed. With the increase in temperature from 25C to 45C the ATPase activity decreased by nearly 80%. The solubility profile of actomyosin in the presence of zinc salts shows a sigmoid pattern as the concentration of both the zinc salts increases. Free SH content of actomyosin decreased with the increase in concentration of zinc salts. Intrinsic fluorescence indicated significant decrease in relative fluorescence intensity of actomyosin. This indicates significant alterations in the structure of actomyosin. Analysis of secondary structure also indicates significant alteration in the [alpha]-helical content upon binding of both zinc salts.

Item Type: Article
Uncontrolled Keywords: Oil sardine Fish actomyosin Solubility Zinc chloride Zinc sulfate ATPase Fluorescence spectra Far UV-circular dichroic spectra
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 03 Proteins
600 Technology > 08 Food technology > 28 Meat, Fish & Poultry
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 17 Jun 2009 11:30
Last Modified: 28 Dec 2011 10:09
URI: http://ir.cftri.com/id/eprint/9053

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