Heat-induced changes in sodium Caseinate

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Abstract
Summary: Chemical and physical changes that occur in Na caseinate (at 1 or 2% in water, pH 7·0) on heating in the range 120–150 °C were investigated by polyacrylamide gel electrophoresis, ion-exchange and gel-permeation chromatography, light scattering, u.v. spectroscopy, amino acid analysis, and the formation of pH 4·6 and 12% TCA-soluble N and 12% TCA-soluble P. The electropherograms of heated samples were smeared and indistinct suggesting intermolecular aggregation which was not reversed by 6 M-urea or SDS and indicating covalent bond formation; αs2-casein was especially sensitive. Aggregation was confirmed by ion-exchange chromatography and light scattering. Fragmentation of the caseins also occurred on heating, as indicated by the formation of pH 4·6 and 12% TCA-soluble N and by gel filtration. Formation of soluble N and dephosphorylation followed first-order kinetics. Concentrations of available lysine and available methionine were reduced by 10–15% on heating at 140 °C for 30min; chemical assays for arginine and tryptophan indicated increases, suggesting interference. Ultraviolet spectroscopy indicated a slight apparent increase in aromatic residues after heating at 140 °C for up to 60 min.