The secretion of amylase, phospholipase and protease from Aeromonas salmonicida, and the correlation with membrane-associated ribosomes

Abstract. The following extracellular enzymes have been readily detected in the culture filtrates from Aeromonas salmonicida: amylase, phospholipase, lysophospholipase and ribonuclease. Amylase and phospholipase have been partially characterized. Evidence suggests that glycogen may be the natural substrate for amylase, and that the role of the enzyme in natural infection is to digest glycogen present in fish muscle. The secretion of amylase activity is suppressed by the addition of glucose to the growth medium. The amounts of amylase, phospholipase and protease that can be detected in culture filtrates decreases with increase in the growth temperature from 25 to 32°C. This marked decrease in secretion of hydrolytic enzymes occurs although the initial growth rates at 25 and 32°C are similar. Free and membrane associated ribosomes have been isolated from cultures grown at 25 and 32°C. At 32°C there is a smaller proportion of membrane-associated ribosomes and this is consistent with the hypothesis that extracellular enzymes from Aeromonas salmonicida are secreted on membrane-bound polysomes.