4.6 Article Proceedings Paper

Study of the protein-bound fraction of calcium, iron, magnesium and zinc in bovine milk

Journal

SPECTROCHIMICA ACTA PART B-ATOMIC SPECTROSCOPY
Volume 56, Issue 10, Pages 1909-1916

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/S0584-8547(01)00313-5

Keywords

milk; casein; trichloroacetic acid; pepsin; ICPOES

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Two approaches were used to study the interaction of Ca, Fe, Mg and Zn with bovine milk proteins by inductively coupled plasma optical emission spectrometry (ICPOES). Selective separations in bovine milk samples were accomplished employing an acid protein precipitation using 100 g l(-1) trichloroacetic acid (TCA), and an enzymatic protein hydrolysis using 50 g l(-1) pepsin (PEP) solution, respectively. The results were compared with total mineral contents determined after microwave-assisted acid digestion. The results obtained by enzymatic and acid precipitation evidenced the different interaction forms of Ca, Fe, Mg and Zn in the system formed by milk components. Iron was not solubilized by the TCA treatment, but was recovered completely after the enzymatic treatment. Quantitative recoveries of Ca, Mg and Zn were obtained using both approaches, showing that these analytes were bound to milk compounds affected by either treatment. Calcium, Mg and Zn are mainly associated with colloidal calcium phosphate and Fe is bound to the backbone of the casein polypeptide chain, cleaved by pepsin enzyme. The proposed approaches could be used to assess the complexity of these chemical interactions. (C) 2001 Elsevier Science B.V rights reserved.

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