Proteolytic activity of Aeromonas caviae.
Aeromonas strains produce a variety of virulence factors including proteases. Studies on the kinetics of growth of Aeromonas caviae NRRL B-966 and its proteases suggest that the proteolytic activities are produced throughout the growth phase, with peak level occurring at stationary phase. A. caviae synthesize both intracellular and extracellular proteases with the latter account for major portion of the total activity. Optimum pH for the A. caviae proteolytic activity is at 7.0. A. caviae produces a thermoresistant protease, whose activity is dependent on Mg++ and Ca++ ions. Inhibition of proteolytic activity by phenyl methyl sulfonyl fluoride suggest the presence of a serine protease in A. caviae. Nitrogenous compounds enhance the proteolytic activity while carbohydrates tested in this study inhibit the activity.
D000333:Aeromonas / Q000254:growth & development / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D002413:Cations, Divalent / Q000737:chemistry; D004229:Dithiothreitol / Q000737:chemistry; D004492:Edetic Acid / Q000737:chemistry; D019286:Endopeptidase K; D010450:Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010664:Phenylmethylsulfonyl Fluoride / Q000737:chemistry; D012697:Serine Endopeptidases / Q000378:metabolism; D013696:Temperature; D013997:Time Factors
D001426:Bacterial Proteins; D002413:Cations, Divalent; D010664:Phenylmethylsulfonyl Fluoride; D004492:Edetic Acid; D010450:Endopeptidases; D012697:Serine Endopeptidases; D019286:Endopeptidase K; D004229:Dithiothreitol