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Appl Environ Microbiol. 1970 April; 19(4): 586-588
Copyright © 1970 American Society for Microbiology. All Rights Reserved.

Naphthylamidase Activity of Leptospira¹

Department of Veterinary Microbiology, School of Veterinary Medicine, University of Missouri, Columbia, Missouri 65201
Department of Microbiology, School of Medicine, University of Missouri, Columbia, Missouri 65201

ABSTRACT

Extracts of 18 serotypes of the genus Leptospira were found to possess naphthylamidase activity, and differences in the pathogenic and saprophytic strains were noted. The former exhibited a preference for the leucyl naphthylamide substrate, whereas the latter demonstrated greater hydrolysis of alanyl naphthylamide. With the leucyl naphthylamide as substrate, pathogenic strains showed 10 to 20 times higher naphthylamidase activity than saprophytic strains. Optimal temperature and pH for enzymatic hydrolysis also differed between pathogenic and saprophytic strains. Maximal enzymatic activities for pathogenic and saprophytic naphthylamidases were 41 and 37 C, respectively, at pH 8.0 to 8.5. The pH and temperature optima suggested that the leptospiral enzyme activity was not leucine aminopeptidase.

¹ Work done by G. B. in partial fulfillment of the degree of Master of Science in Public Health. This study was supported by a public health traineeship from the Public Health Service, U.S. Department of Health, Education, and Welfare.