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Isolation and characterisation of two extracellular metalloproteases from Aeromonas salmonicida ssp. salmonicida
Author(s) -
Arnesen J. A.,
Eggset G.
Publication year - 1999
Publication title -
journal of fish diseases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.819
H-Index - 85
eISSN - 1365-2761
pISSN - 0140-7775
DOI - 10.1046/j.1365-2761.1999.00135.x
Subject(s) - aeromonas salmonicida , aminopeptidase , metalloproteinase , extracellular , enzyme , biology , molecular mass , biochemistry , leucyl aminopeptidase , leucine , microbiology and biotechnology , hydrolysis , phenylalanine , bacteria , amino acid , genetics
Two extracellular metalloproteases were purified from a culture filtrate derived from Aeromonas salmonicida ssp. salmonicida . One enzyme, leucine aminopeptidase (LAP), which had a molecular mass 37 kDa, hydrolysed aminoterminal l ‐leucine and l ‐phenylalanine. The activity was inhibited by 1,10‐o‐phenanthroline, but not by EDTA. The addition of excess Zn 2+ to an o‐phenanthroline‐inhibited enzyme restored most of its activity. The peptidase was temperature stable, and had an optimum temperature and pH of 60 °C and 8, respectively. The other enzyme, metalloprotease 3 (MP3), which had a molecular mass 20 kDa, was an endoprotease, and hydrolysed azocoll and hide powder‐azure, but not gelatine. The MP3 enzyme had an optimum temperature and pH of ≈40 °C and 7.5, respectively, and a cationic isoelectrical point.