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A simple quantitative plate assay was used to study the proteolytic activity of Aeromonas hydrophila complex. All the A. hydrophila complex strains hydrolyzed albumin, casein, and fibrinogen; most of the strains also digested gelatin (99.9 %), hemoglobin (94.3%), and elastin (73.2 %). None of the strains hydrolyzed collagen. The activity on each substrate varied from isolate to isolate. By using correlation analysis a close relationship was obtained among these proteolytic reactions, especially with albumin, casein, fibrinogen, gelatin, and hemoglobin hydrolysis. The elastin hydrolysis demonstrated a lower correlation with the other 5 proteolytic activities and implied a different enzymatic system. A higher casein and elastin hydrolytic response was found in the strains derived from human, fish, and other animal sources than those from water environments.
Shotts et al. (Tue,) studied this question.