Dl. Vanhekken et Ed. Strange, RHEOLOGY AND MICROSTRUCTURE OF CHEMICALLY SUPERPHOSPHORYLATED WHOLE CASEIN, Journal of dairy science, 80(11), 1997, pp. 2740-2750
Whole bovine casein was chemically modified using POCl3 to contain 9.1
, 10.6, and 12.5 mmol of bound P/mmol of casein [(160, 190, and 220% P
, respectively) relative to the 5.6 mmol of P/mmol of unmodified casei
n (100% P)]. Superphosphorylation produced two types of modified casei
ns. Solutions made with 220% P casein had low viscosities, which remai
ned constant between pH 5 and 9 and between protein concentrations of
0.2 and 0.7%; these solutions remained fluid when exposed to up to 30
mM Ca2+. Solutions made with 160 or 190% P caseins increased in viscos
ity as protein concentration and pH increased; the solutions formed ge
ls at 1% protein, which increased in elastic modulus, viscous modulus,
and complex viscosity as the protein and Ca2+ concentrations increase
d. When exposed to Ca2+, gels became more curd-like as protein aggrega
ted and then underwent syneresis. Electron microscopy showed that the
gel microstructure consisted of an open matrix of folded strands and s
heets of casein in irregular sizes that condensed upon exposure to Ca2
+. These unique interactions among proteins and unique rheological pro
perties suggest that superphosphorylation could be useful in creating
novel dairy foods with added value and enhanced functionality.