Portal de Periódicos da CAPES

Micellisation of β-casein

2002; Elsevier BV; Volume: 210; Issue: 2-3 Linguagem: Inglês

10.1016/s0927-7757(02)00371-0

1873-4359

C. G. de Kruif, V. Ya. Grinberg,

Phytase and its Applications

We measured the dynamic (DLS) and static (SLS) light scattering behaviour of β-casein solutions in a 25 mM Na phosphate buffer at neutral pH as a function of temperature. At low temperatures (0 °C) β-casein is predominantly in a monomer state. With rising temperature micelles are formed with a (concentration-dependent) transition temperature in the range 15–30 °C. The transition is accompanied by a clear positive excess heat capacity. In DLS we observe two relaxation modes. The fast mode is attributed to the diffusive motion of the micelles and leads to a hydrodynamic radius of about 12 nm. The slow mode cannot be attributed to 'physical' particles. It is attributed to polydispersity or equivalently to long-range concentration fluctuations as proposed by Leclerc and Calmettes [15], [16]. From SLS measurements we obtained the molecular mass and divided by the mass of a monomer (24 kDa) it gives the micellisation number, which seems to level off to about 30 at 40 °C. The measured micellisation number is predicted quite satisfactorily from a thermodynamic model for the calorimetric data as developed by Mikheeva et al. [26] and based on the shell model of Kegeles [24], [25].