Sugars stabilise proteins against extremes of pH and heat denaturation. Thi
s was studied by means of density, ultrasonic velocity and viscosity measur
ements of the following systems (il) ovalbumin-phosphate buffer (pH 2.4, 5.
2, 7.0 and 8.9) and (ii) ovalbumin-maltose-phosphate buffer (pH 2.4, 5.2, 7
.0 and 8.9) systems as functions of concentration and temperature. The part
ial specific volumes (<(<nu>)over bar>(0)), partial specific adiabatic comp
ressibility (<(<beta>)over bar>(s)), intrinsic viscosity, [eta] and shape f
actor, nu, were calculated for the said systems. The results obtained from
such studies suggest that the stabilisation of ovalbumin occurs in the pres
ence of maltose through strengthening of hydrophobic interactions. (C) 2001
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