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

H.F.M. Hermes, T. Sonke, P.J.H. Peters, J.A.M. Balken, van, J. Kamphuis, L. Dijkhuizen, E.M. Meijer

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Abstract

An L-aminopeptidase of Pseudomonas putida, used in an industrial process for the hydrolysis of D,L-amino acid amide racemates, was purified to homogeneity. The highly L-enantioselective enzyme resembled thiol reagent-sensitive alk. serine proteinases was strongly activated by divalent cations. It possessed a high substrate specificity for dipeptides and a-H amino acid amides, e.g., L-phenylglycine amide. [on SciFinder (R)]
Original languageEnglish
Pages (from-to)4330-4334
JournalApplied and Environmental Microbiology
Volume59
Issue number12
Publication statusPublished - 1993

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