Partial purification and characterization of aminopeptidase from debittering and non-debittering strains of Lactobacillus casei ssp. were undertaken. The aminopeptidase activity of both strains was optimal at pH 7.0 and at 40-degrees-C. The enzymes were strongly inactivated by EDTA and 1:10 phenanthroline and activated by bivalent cations Co++ and Mg++. The aminopeptidase of a debittering strain showed a much broader substrate specificity when compared to the non-debittering strain.