Some properties of β-casein modified via phosphatase

Darewicz, M. and Dziuba, J. and Minkiewicz, P. (2005) Some properties of β-casein modified via phosphatase. Acta Alimentaria, 34 (4). pp. 403-415. ISSN 0139-3006

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Abstract

Modifiedß-casein forms were prepared with acid/alkaline phosphatase. The choice between acid and alkaline phosphatases was critical for the physico-chemical properties ofß-casein. Removal of phosphoryl groups fromß-casein via alkaline phosphatase increased the retention time measured using RP-HPLC and did not change the second-derivative UV spectra. Moreover, the pI value shifted to neutral pH and the solubility decreased, especially at the alkaline pH range.ß-Casein modified enzymatically via alkaline phosphatase formed a foam with volume and stability similar to that formed with intact one. In turn, a dramatic decrease in foam stability was found forß-casein modified via acid phosphatase. Chromatographic, spectral and electrophoretic results suggest proteolytic acivity of acid phosphatase preparation.

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