Pressure-induced dissociation of casein micelles: size distribution and effect of temperature.
Pressure-induced dissociation of a turbid solution of casein micelles was studied in situ in static and dynamic light scattering experiments. We show that at high pressure casein micelles decompose into small fragments comparable in size to casein monomers. At intermediate pressure we observe particles measuring 15 to 20 nm in diameter. The stability against pressure dissociation increased with temperature, suggesting enhanced hydrophobic contacts. The pressure transition curves are biphasic, compatible with a temperature (but not pressure)-dependent conformational equilibrium of two micelle species. Our thermodynamic model predicts an increase in structural entropy with temperature.
Gebhardt
R
R
Physics Department E13, Technical University Munich, Garching, Germany.
Doster
W
W
Kulozik
U
U
D002364:Caseins / Q000737:chemistry*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D006874:Hydrostatic Pressure; D008027:Light; D008823:Micelles; D008956:Models, Chemical; D010446:Peptide Fragments / Q000737:chemistry; D012542:Scattering, Radiation; D013816:Thermodynamics
D002364:Caseins; D008823:Micelles; D010446:Peptide Fragments