Structure of the casein micelle. A proposed model

Abstract

Summary: On the basis of complete permeability by high molecular weight reagents of casein micelles in milk and a uniform distribution of the 3 different casein subunits, a model of the micelle structure is proposed. It is composed of an average repeating unit of 1 κ-, 2 α_s1;- and β-casein subunits assembled in a 3-dimensional network or branched polymer made of 130–130000 monomers, in which the trimers of κ-casein occupy the nodes and the copolymers of α_s1;- and β-caseins make up the branches. All the associations between subunits are through non-covalent bonds. The chemical composition varies with the number of α_s1;- and β;-casein subunits in the branches. This proposed structure is strongly supported by evidence from electron microscopy and a scale model has been made. It leads to an understanding of the role of κ-casein in micelle formation and opens new perspectives in explaining some properties of the caseins. It offers an interesting example of a new type of quaternary structure of protein subunits.