Prabrisha Chatterjee*
Background: Milk proteins are a rich source of peptides which are bioactive. Beta Casomorphin-7 (BCM-7) is produced by successive proteolytic ingestion of beta- casein variants A1 and B, while not observed in A2 variant. The large amount of proteins in bovine’s milk are caseins, which consist of four categories (αs1, αs2, β, and κ) encrypted by corresponding genes (CSN1S1, CSN1S2, CSN2, and CSN3, respectively). Ingestion of A1 beta-casein showed the way for the emergence of Beta Casomorphin-7 (BCM-7), a peptide that has been proposed to be a major cause of various human hazards.
Result: The relative profuseness of proline, methionine, and α-lactose were the highest in A2 variant of β-casein, while glycine, citric acid, choline, and cAMP (cyclic Adenosine Monophosphate) exhibited the highest abundance in A1 variant. These results thus come up with novel insights into the effect of casein variants, further expediting research into the biogenesis of milk ingredients and the prospective physiological activity of milk correlated with variants of β-casein.