[Relationship between thermal treatments of milk and molecular hysteresis of the milk protein system (author's transl)].
The potentiometric titration curve of milk does not show an equilibrium curve but a hysteresis loop between pH 6.2 und pH 4.8. Hysteresis means thermodynamic metastability and cooperative changes within a structural domain. The structural domain involved in these changes is the casein micelle. Cooperative conformation changes and thermodynamic metastability appear on the resolution of the casein micelle caused by the action of protons. The charge condition of the polypeptide chains is not synchron with the charge supply. The lag depends on the thermal treatment. Therefore the milk protein system can serve as a memory for physical datas.
D000818:Animals; D002364:Caseins / Q000032:analysis; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008892:Milk / Q000032:analysis*; D008894:Milk Proteins / Q000032:analysis*; D011199:Potentiometry; D013816:Thermodynamics
D002364:Caseins; D008894:Milk Proteins
Zusammenhänge zwischen thermischer Behandlung der Milch und molekularer Hysteresis des Milchproteinsystems