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Binding of Ca(II) by the 11S fraction of soybean proteins.

Appu Rao, A. G. and Rao, M. S. N. (1975) Binding of Ca(II) by the 11S fraction of soybean proteins. Cereal Chemistry, 52 (1). 21-33, 22 ref..

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Abstract

Binding of Ca(Il) by the l1S fraction of soybean proteins was determined by equilibrium analysis at pH 7.8 and 5.5. The binding was negligible at pH 5.5. At pH 7.8 binding was increased by the addition of 0.5 M NaC!. Prior treatment with EDTA also reduced the binding. Analysis of the binding data with the Scatchard equation suggested that the probable binding site on the protein molecules was the imidazole group. Addition of CaII did not cause association or dissociation of the protein. Heat coagulation was increased by the addition of Ca(II). The protein was almost quantitatively precipitated at 1.0 x 1O-2 M Ca(II). This precipitation was decreased by the addition of NaCl. Binding studies with the unfractionated soybean proteins indicated that Ca(ll) was bound by the proteins as well as the phytate impurities. When these were removed Ca(II) appeared to be bound by the proteins at the imidazole group.

Item Type: Article
Uncontrolled Keywords: Soybean proteins, 11s proteins, calcium
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: 13 Jul 2016 10:28
Last Modified: 13 Jul 2016 10:28
URI: http://ir.cftri.com/id/eprint/3153

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