Search
Filter Results
- Resource Type
- Article1
- Book1
- Book Print1
- Journal1
- Article Type
- English Abstract1
- Result From
- Lane Catalog1
- PubMed1
- SearchWorks (biomedical subset) 1
-
Year
- Journal Title
- Z Lebensm Unters Forsch1
Search Results
Sort by
- JournalDigital Access Silverchair v.1-, 1979-CME NOT INCLUDED with institutional subscriptions.
- ArticleKrichmeier O.Z Lebensm Unters Forsch. 1976;160(3):293-8.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.