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Modulation of physico-chemical properties of bovine β-casein by nonenzymatic glycation associated with enzymatic dephosphorylation

Darewicz, M. and Dziuba, J. and Mioduszewska, H. and Minkiewicz, P. (1999) Modulation of physico-chemical properties of bovine β-casein by nonenzymatic glycation associated with enzymatic dephosphorylation. Acta Alimentaria, 28 (4). pp. 339-354. ISSN 0139-3006

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Abstract

A major bovine casein fraction, β-casein was chemically glycated and/or enzymatically dephosphorylated. Ten glucose and nine lactose moieties were attached while all phosphate groups were removed. Glycation shifted the pI to acidic pH range and decreased the solubility at acidic pHs while dephosphorylation shifted the pI to neutral pH range and increased the solubility at acidic pHs. Dephosphorylation led to longer retention time measured using the reversed-phase high-performance liquid chromatography and affected UV-spectra of β-casein which suggested structural changes. Glycation did not affect these properties. Both modifications decreased the calcium sensitivity of β-casein, making it to keep αS1-casein in solution in the presence of Ca2+.

Item Type: Article
Subjects: Q Science / természettudomány > QD Chemistry / kémia > QD01 Analytical chemistry / analitikai kémia
Depositing User: xKatalin xBarta
Date Deposited: 23 Feb 2017 12:09
Last Modified: 30 Nov 2019 00:27
URI: http://real.mtak.hu/id/eprint/49596

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