BIOMOLECULES AND ENZYMES

Detailed explanation-1: --Casein is the most hydrophobic casein and has a highly charged N-terminal domain, containing an anionic phosphoserine cluster, that is clearly distinct from a very hydrophobic C-terminal domain (Swaisgood, 2003).

Detailed explanation-2: -S‐Caseins are the major casein proteins with 8–12 seryl phosphate groups, while ‐casein contains about 5 phosphoserine residues and is more hydrophobic than S‐caseins and k‐casein [49].

Detailed explanation-3: -Milk: Sources and Composition -Casein has four variants, A, B, C, and D, of which B is the most common. Its polypeptide chain has three distinct regions that are strongly hydrophobic. It is highly negatively charged, while the rest of the molecule is essentially neutral.

Detailed explanation-4: -Caseins are mammalian milk proteins with a loose tertiary, highly hydrated structure. They possess clusters of phosphoserine and phosphothreonine residues that bind amorphous calcium phosphate, which allows milk to contain higher levels of soluble calcium than is possible in ordinary solutions.

Detailed explanation-5: --Casein, an amphiphilic molecule with only one phosphoseryl residue, has charged trisaccharide or tetrasaccharide moieties located in the C-terminal segment. The rest of the molecule, however, is highly hydrophobic in character.