Journal Article


Mark A Fenelon
James A O'Mahony
Alan L Kelly
Noel A McCarthy


Agriculture & Food Science

electrophoresis polyacrylamide gel acid phosphatase human calcium casein bovine physical properties water

The physical characteristics and emulsification properties of partially dephosphorylated bovine β-casein. (2012)

Abstract Bovine β-casein was purified from phosphocasein by rennet coagulation and cold solubilisation from the resultant curd. β-Casein was then dephosphorylated using potato acid phosphatase. Urea-polyacrylamide gel electrophoresis (PAGE) of partially dephosphorylated β-casein showed a number of bands, depending on the final level of phosphorylation. Dephosphorylating β-casein increased its pH of minimum solubility from ∼pH 5 to 5.5 and reduced its net negative charge from -30.8 to -27.0mV. During the acidification of β-casein solutions, partially dephosphorylated β-casein failed to form a gel, unlike the phosphorylated (i.e., control) β-casein. Use of partially dephosphorylated β-casein to stabilise oil-in-water emulsions resulted in larger fat globules compared to control β-casein, but such globules were less susceptible to aggregation in the presence of 15 or 30mM CaCl(2). Overall, the dephosphorylation of β-casein resulted in a protein similar to human β-casein in terms of physicochemical functionality, with increased stability against calcium-induced aggregation.
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Full list of authors on original publication

Mark A Fenelon, James A O'Mahony, Alan L Kelly, Noel A McCarthy

Experts in our system

M A Fenelon
Total Publications: 28
James A. O'Mahony
Total Publications: 34
Alan L. Kelly
Total Publications: 63
Noel McCarthy
Total Publications: 9