Reduction of allergenicity and increasing the biological value of buffalo's milk proteins by enzymatic modification
1996
Hussein, S. | Gelencser, E. | Hajos, Gy
Buffalo milk proteins were covalently enriched with methionine (Met) during the enzymatic peptide modification (EPM) process. The maximal Met-enrichment occurred when the alpha-chymotryptic hydrolysate of buffalo's milk proteins was treated with methionine ethyl ester in the presence of alpha-chymotrypsin during the EPM. Methionine content of this product was more than three times (5.4%) higher than that of the original buffalo milk protein (1.5%). The electrophoretic patterns of the modified proteins showed that the enzymatic reaction was mainly characterized by transpeptidation. Molecular masses of the modified protein fractions were influenced by the concentration of L-methionine ethyl esters in the reaction mixture during the EPM. EPM products from the buffalo milk protein hydrolysates with alpha-chymotrypsin and trypsin or with pepsin and trypsin showed low allergenic activities compared with those when buffalo milk proteins were hydrolyzed with alpha-chymotrypsin or with pepsin alone.
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