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. 1980 Nov;40(5):876–882. doi: 10.1128/aem.40.5.876-882.1980

Purification and Partial Characterization of an Aminopeptidase from Lactobacillus lactis

Bernhard Eggimann 1,†, Marc Bachmann 1
PMCID: PMC291682  PMID: 16345655

Abstract

A surface-bound aminopeptidase of Lactobacillus lactis cells was solubilized with lysozyme, and the extract was subjected to streptomycin sulfate precipitation, ammonium sulfate fractionation, chromatography on Sephadex G-100 and diethylaminoethyl-Sephadex A-50, and preparative polyacrylamide gel electrophoresis. The purified enzyme was homogeneous in disc electrophoretic analysis and consisted of a single polypeptide chain with a molecular weight of 78,000 to 81,000. The optimal pH and optimal temperature for enzyme activity were 6.2 to 7.2 and 47.5°C, respectively, for l-lysine-4-nitroanilide as the substrate. The enzyme was activated by Co2+ and Zn2+ ions and inhibited by Cu2+, Hg2+, and Fe3+ ions and by the metal-complexing reagents ethylenediaminetetraacetic acid, 1,10-phenanthroline, and α,α′-dipyridyl. Higher concentrations of substrate and hydrolysis products also inhibited the activity of the enzyme. The aminopeptidase had broad substrate specificity and hydrolyzed many amino acid arylamides and many peptides with unsubstituted NH2-terminal amino acids.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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