Search results for "Caseinase"
showing 3 items of 3 documents
Secretion of haemolysins and proteases by Aeromonas hydrophila EO63: separation and characterization of the serine protease (caseinase) and the metal…
2004
C . E S T E V E A N D T . H . B I R K B E C K . 2004. Aims: To determine the haemolysins and proteases excreted by the virulent strain EO63 of Aeromonas hydrophila grown in complex media and to then fractionate and characterize them, in particular those with elastolytic activity. Methods and Results: The amount of haemolytic and proteolytic activity in EO63 culture supernatants was dependent on the culture media used. In all media, haemolysins appeared during the phase of active growth and haemolytic activity decreased quickly thereafter, as previously described for aerolysin. In contrast, proteases were mainly released during the stationary phase. Serine protease activity in EO63 culture s…
Probiotic properties of Brevibacillus brevis and its influence on sea bass (Dicentrarchus labrax) larval rearing
2012
Efficacy of Brevibacillus brevis strain and its influence on larval rearing of sea bass (Dicentrarchus labrax) were investigated in the present work. Biochemical analyses permit to identify this strain as B. brevis. This bacterium has an inhibitory effect against fish pathogenic bacteria, especially the genus of Vibrio. Enzymatic characterization revealed that B. brevis was lipase positive, amylase, lecithinase and caseinase negative. Adherence assays to abiotic surfaces and challenge test with Artemia larvae demonstrate that B. brevis was fairly adherent and play an important role in the enhancement of the protection of Artemia culture against pathogens. Treatment of sea bass larvae with B…
Toxicity of the extracellular products ofVibrio damsela isolated from diseased fish
1993
In this work we analyzed the pathogenic in vivo and in vitro activities for both fish and mammals of extracellular products (ECP) of several isolates of Vibrio damsela implicated in disease problems in marine culture. The ECP from all the strains were strongly lethal for fish (LD50 ranging from 0.06 to 3.7 μg protein/g fish) and mice (LD50 ranging from 0.02 to 0.43 μg protein/g mouse), causing death between 4 and 72 h after inoculation. These ECP samples possessed low proteolytic activity without production of caseinase, gelatinase, or elastase. However, most of them showed remarkable phospholipase and hemolytic activity for sheep, human, and turbot red blood cells. In addition, all the ECP…