Pressure-induced dissociation of casein micelles: size distribution and effect of temperature
Braz. j. med. biol. res
;
38(8): 1209-1214, Aug. 2005. ilus, tab, graf
Article
in English
| LILACS
| ID: lil-405522
RESUMO
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.
Full text:
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Index:
LILACS (Americas)
Main subject:
Caseins
/
Micelles
Type of study:
Prognostic study
Language:
English
Journal:
Braz. j. med. biol. res
Journal subject:
Biology
/
Medicine
Year:
2005
Type:
Article
/
Congress and conference
Affiliation country:
Germany
Institution/Affiliation country:
Department for Food and Nutrition/DE
/
Technical University Munich/DE
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