DEBITTERING OF PROTEIN HYDROLYSATES USING AEROMONAS-CAVIAE AMINOPEPTIDASE

The bitter-tasting peptide solutions prepared from the protease hydrol ysate of milk casein and soy protein were treated with aminopeptidase produced by Aeromonas caviae T-64. The bitterness of these solutions w ere significantly reduced with an increase in the amount of released f ree amino acids. Hydrophobic amino acids having Delta fvalues more tha n 1500 cal/mol, such as Saline, isoleucine, leucine, tyrosine, and phe nylalanine, accounted for more than 76% of the free amino acids releas ed by the aminopeptidase. The results suggest that the enzyme hydrolyz ed bitter peptides containing hydrophobic amino acids in the N-termina l region and the bitterness of the peptides were reduced by removal of these amino acids.