Effect of sucrose on molecular and interaction parameters of sodium caseinate in aqueous solution: relationship to protein gelation

The effect of sucrose on molecular and interaction parameters of sodium caseinate in aqueous medium has been investigated using static and dynamic multi-angle laser light scattering over a wide range of sucrose concentration (from 10 to 78 w/v%) and pH values (from 7.0 to 3.5). Measurements have been made of the molar mass, the radius of gyration, the hydrodynamic radius, and the second virial coefficient of sodium caseinate in aqueous solution. Pronounced dissociation of sodium caseinate sub-micelles¹ was found in the presence of sucrose at a pH above the protein's isoelectric point. The effect of sucrose at a pH near the isoelectric point is very different. This is reflected in the pronounced increase in molar mass, radius of gyration, and the difference between the radius of gyration and the hydrodynamic radius. It was found that the extent of the protein association, caused by the presence of sucrose, is a key factor contributing to the hydrophobic–hydrophilic balance of the protein surface, and hence to the thermodynamic affinity of the caseinate sub-micelles for the aqueous medium and for each other. Analysis of light-scattering data using structure-sensitive plots shows a clear transition from Gaussian to wormlike chain/rod behaviour for sodium caseinate on pH lowering. Apparent relationships between the effects of sucrose on the self-association of sodium caseinate and a marked enhancement of the viscoelasticity of acid-induced casein gels have been revealed. Moreover, the dissociation of sodium caseinate sub-micelles is in excellent agreement with the more homogeneous microstructure of acid-induced protein gels in the presence of sucrose as detected by confocal laser scanning microscopy. We discuss likely molecular mechanisms underlying the observed effects of sucrose on the interactions and rheology in acidified caseinate systems.