Solubility Solvation, and Stabilization of αs1 - and β-Caseins

Abstract

asl-Casein A has been observed to differ from a,~-B by its solubility in CaCI~ solutions at 1 and 37 C, and by its stabilization profile in the presence of K-casein and calcium ions. The different characteristics of the protein a~-A have been attributed to the deletion of a segment of nonpolar amino acids resulting in decreased hydrophobic interactions among a~l-A molecules. The deletion also has impaired the formation of a~l-K-casein micelles under conditions of normal formation.