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A chitinase was identified in extracellular products of a virulent Aeromonas hydrophila isolated from diseased channel catfish (Ictalurus punctatus). Recombinant chitinase (rChi-Ah) was produced in Escherichia coli. Purified rChi-Ah had optimal activity at temperature of 42˚C and pH 6.5. The affinity (Km) for chitosan was 4.18 mg•ml −1 with Vmax of 202.5 mg•min −1 •mg −1 . With colloidal chitin as substrate, rChi-Ah generated N,N'-diacetyl-glucosamine predominantly. Conversion of chitosan (≥75%doi:10.4236/aim.2015.59064 fatcat:bupts7yuqnafldlrda5p3bj4ki