Abstract
Abstract.Traditional biochemieal techniques and a stain to detect proteases in polyacrylamide gels were used to identify and partially characterize three proteases, P1, P2 and P3, produced byAeromonas hydrophilastrain Ah 22. P1 was found to be a heat‐labile serine protease with an optimum pH of 7·5, while P2 is a heat‐stable metalloprotease with an optimum pH of 8·0, and P3 is a moderately heat‐stable metalloprotease with peak activity beween pH 7 and 11. A comparison of 17 other strains of theA. hydrophilacomplex indicated that four produced P1, P2 and P3. Two strains produced just P1 and P3; one produced only P3; six produced two different serine proteases, P2a and P2b; and two produced a number of uncharacterized proteases. Virulence studies in age‐0 + channel catfish indicated no correlation between either quantitative or qualitative protease production and virulence.
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