文摘
The role of 尾-casein as a molecular chaperone in modifying the aggregation of 尾-lactoglobulin was investigated. Using size-exclusion chromatography coupled with a multi-angle laser light scattering detector and dynamic light scattering, it was found that the size of the aggregates formed when 尾-casein was present was reduced. Transmission electron microscopy images showed that 尾-casein & 尾-lactoglobulin mixtures produced smaller globular aggregates, with more uniform size distribution, than 尾-lactoglobulin alone. The viscosity of the solutions after heat treatment was minimally altered by the presence of 尾-casein. The surface hydrophobicity of the aggregates formed when 尾-casein was present did not differ from those formed in 尾-lactoglobulin. 尾-Casein was present in all the aggregate fractions in significant quantities, suggesting the formation of mixed 尾-casein-尾-lactoglobulin aggregates with a lower propensity for growth or forming secondary aggregates.