Life SciencesBiochemistryGlycobiologyMilk ChemistryProtein BiochemistryCasein ChemistryGlycan AnalysisMilk ProteinsAmino Acid Composition AnalysisCasein DenaturationCasein ModificationGlycopeptide Identification
The main casein components were somewhat degraded when sterilized. The hydrolytic action of heat is not the same as that of rennin. However, for K-casein, the actions of rennin and of heat (120 C--20 rain) seem to be similar. A heat caseinoglyeopeptide was isolated and it had nearly the same amino acid composition as the rennin caseino-glycopeptide. These data again suggest the existence of a very labile linkage in K-casein which was easily split by different procedures.
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Preparation of β-casein by a modified urea fractionation method
R. Aschaffenburg · Journal of Dairy Research · 1963 · 112 citations
Agriculture, Biochemistry, Genetics +12