Purification and characterization of an L-aminopeptidase from Pseudomonas putida ATCC 12633

Abstract

An L-aminopeptidase of Pseudomonas putida, used in an industrial process for the hydrolysis of D2L-amino acid amide racemates, was purified to homogeneity. The highly L-enantioselective enzyme resembled thiol reagent- sensitive alkaline serine proteinases and was strongly activated by divalent cations. It possessed a high substrate specificity for dipeptides and α-H amino acid amides, e.g., L-phenylglycine amide.