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 language | English |
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Pages (from-to) | 4330-4334 |
Journal | Applied and Environmental Microbiology |
Volume | 59 |
Issue number | 12 |
Publication status | Published - 1993 |