Characterization of proteases produced by virulent strain of Aeromonas

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The properties of metalloprotease produced by A. hydrophila and of serine protease produced by A. trota were examined. A. hydrophila produces the metalloprotease as the intermediate form, which is composed of mature domain and carboxy-terminal domain, into milieu. The intermediate form released into milieu is immediately cleaved to remove the carboxy-terminal domain and turns into mature form. To clear the property of the intermediate form, we constructed the plasmid harboring metalloprotease gene and introduced it into Escherichia coli. The examination of the metalloprotease produced by the transformed cell showed that the intermediate form is not detected, though the mature form is detected.Subsequently, I showed that A. trota produced much amount of serine protease at 25 degree than at 37 degree and that the addition of skim milk in the medium promoted the production of serine protease by A. trota.