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Interaction Of Zn(II) With Bovine Milk A-Casein: Structure–Function Study

Srinivas, S. and Prakash, V. (2011) Interaction Of Zn(II) With Bovine Milk A-Casein: Structure–Function Study. Journal of Food Biochemistry , 35. pp. 1311-1326.

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Abstract

a-Casein is the major casein from bovine milk, responsible for binding to metal ions. Interaction of a-casein with Zn(II) studied by equilibrium dialysis indicates the presence of 17.0 � 2.0 binding sites for Zn(II) with two association constants ka1 0.2 � 0.03 ¥ 106 M–1 and ka2 2.7 � 0.3 ¥ 106 M–1, respectively. Far-Ultraviolet Circular dichroic measurement shows formation of secondary structures in the presence of Zn(II). Fluorescence quenching studies by acrylamide shows blue shift in the emission maxima and decreased Stern– Volmer constant from 10.4 to 4.1 M-1. The kinetics of binding as analyzed by stopped flow shows pseudo-first-order rate of 37 � 5 s-1. Holistically, this interaction leads to formation of stable complexes, useful for fortification of milk-based products with micronutrient zinc.

Item Type: Article
Uncontrolled Keywords: a-Casein; bovine milk; Zn(II); micronutrient
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 03 Proteins
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 05 Aug 2011 11:21
Last Modified: 28 Dec 2011 10:28
URI: http://ir.cftri.com/id/eprint/10416

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