Methionine Enrichment of Milk Protein by Enzymatic Peptide Modification

Methionine-enriched protein was produced from an enzymatically pre-hydrolyzed milk protein using an enzymatic peptide modification (EPM) method with α-chymotrypsin as catalyst. Methionine of the product was twice as high as that of the substrate protein. The incorporated methionine formed a covalent bond with the peptide chain in the product protein. The change in the number of peptide bonds was monitored by the degree of hydrolysis (DH). The slight change of the DH values revealed that a portion of the free amino acids was bound to the peptide chains during the reaction and that transpeptidation was the main process during the EPM treatment. The location of the newly incorporated amino acids was determined by identification of the terminal amino acids. The covalently bound methionine was located in C- and N-terminal positions in a ratio of 3:1.