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. 2001;46(6):515-8.
doi: 10.1007/BF02817995.

Production, purification and characterization of intracellular alanylaminopeptidase of Pseudomonas sp

U Jankiewicz  1 , W Bielawski
Affiliations

Production, purification and characterization of intracellular alanylaminopeptidase of Pseudomonas sp

U Jankiewicz et al. Folia Microbiol (Praha). 2001.

Abstract

The soil bacterium Pseudomonas sp. was found to synthesize an aminopeptidase that prefers Ala-beta-naphtylamide as substrate. The enzyme was purified 660-fold by ammonium sulfate fractionation, preparative electrophoresis, ion exchange chromatography on Protein-Pak Q 8 HR and molecular sieving chromatography on Zorbax SE-250. When purified to homogeneity, the enzyme was shown to be a monomeric protein with a molar mass of 65 kDa; it showed a maximum activity at pH 7.5 and 45 degrees C.

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