Enzymatic characterization of three aeromonas species using API Peptidase, API "Osidase," and API Esterase test kits.

Abstract:

:An enzymatic characterization of 16 strains of Aeromonas species including A. hydrophila (7), A. sobria (5), and A. caviae (4) was carried out using API Peptidase (strips numbered 1, 2, 3, 4, 5, and 6); API Esterase and API "Osidase" test strips. A total of 89 substrates was used in the assay and included 59 arylamides (aminopeptides), 10 esters, and 20 carbohydrates. All three species were remarkably uniform in their reactivities. Nineteen (32%) of the arylamide substrates used were hydrolyzed by all three species. Very strong arylamidase activity was displayed by all three species for L-lysine, L-hydroxyproline, L-arginine, L-alanine, L-proline, and L-leucyl-L-alanine. Esterase activity was strongest against caproate (C6), caprylate (C8), nonanoate (C9), and caprate (C10) substrates. Only a limited number of carbohydrate substrates were hydrolyzed; strong N-acetyl-beta-D-glucosaminidase activity was given by all strains. Both A. hydrophila and A. caviae gave strong beta-D-glucosidase reactivities, while A. sobria appeared to be negative for this enzyme. The results of our preliminary study show that some of the enzymes examined may be useful in the identification and differentiation of these species. The API enzyme assays yielded rapid (4 hr) results. The assays were easy to perform, relatively inexpensive and reproducible. The importance of replicate testing and the inclusion of uninoculated (buffer only) controls as part of the assay is emphasized.

authors

Carnahan AM,O'Brien M,Joseph SW,Colwell RR

doi

10.1016/0732-8893(88)90091-0

subject

Has Abstract

pub_date

1988-08-01 00:00:00

pages

195-203

issue

4

eissn

0732-8893

issn

1879-0070

pii

0732-8893(88)90091-0

journal_volume

10

pub_type

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