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

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