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Binding of Ca(II), Mg(II), and Zn(II) by 7S fraction of soybean proteins.

Rao, A. G. A. and Rao, M. S. N. (1976) Binding of Ca(II), Mg(II), and Zn(II) by 7S fraction of soybean proteins. Journal of Agricultural and Food Chemistry, 24 (3). 490-494, 14 ref..

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Abstract

Binding of Ca(ll) or Mg(II) by 7s protein at pH 7.8 appears to occur at the imidazole groups of the histidine residues of the protein molecule. Zn(II) binding at pH 6.5 also occurs at imidazole groups. The 78 protein binds more Ca(ll) or Mg(II) in borate buffer than in Tris·HCI buffer of the same pH. Rate of proteolysis, fluorescence, optical rotatory dispersion, and circular dichroism measurements do not indicate any conformational change in the protein due to metal ion binding. Ca(Il), Mg(Il), or Zn(II) increases the heat coagulation of 7s protein. At room temperature the protein is precipitated to an extent of 40% by Ca(ll), 10% by Mg(lI), and 90% by Zn(II). NaCI (0.5 M) suppresses precipitation by Ca(ll) or Mg(II) and decreases only slightly precipitation by Zn(ll).

Item Type: Article
Uncontrolled Keywords: 7s fraction, soybean proteins, binding ca (II), mg(II), zn (II)
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 03 Proteins
600 Technology > 08 Food technology > 22 Legumes-Pulses > 05 Soya bean
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 14 Jul 2016 10:50
Last Modified: 14 Jul 2016 10:50
URI: http://ir.cftri.com/id/eprint/3154

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