Isolation and characterization of an alginase from mucoid strains of Pseudomonas aeruginosa.
Strains of Pseudomonas aeruginosa which produce an alginate-like slime polysaccharide were shown to also synthesize an intracellular enzyme which can degrade these polysaccharides and the seaweed alginic acids. The enzyme acts as an eliminase introducing delta 4,5 unsaturation into the uronic acid moiety. It appears to be a polymannuronide lyase which degrades the polysaccharides, depending on their uronic acid composition, to a series of oligosaccharides, the smallest of which is a disaccharide. L-Guluronic acid linkages are not split. The Pseudomonas alginase resembles other bacterial alginases and enzymes from molluscs but differs in some important properties, such as extent of degradation and linkage preference. Nonmucoid forms of the organism produce detectable but much lower amounts of enzyme.
D006026:Glycoside Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D009844:Oligosaccharides / Q000032:analysis; D011133:Polysaccharide-Lyases; D011135:Polysaccharides, Bacterial / Q000302:isolation & purification / Q000378:metabolism*; D011550:Pseudomonas aeruginosa / Q000201:enzymology* / Q000302:isolation & purification; D013045:Species Specificity; D014552:Urinary Tract Infections / Q000382:microbiology
D009844:Oligosaccharides; D011135:Polysaccharides, Bacterial; D006026:Glycoside Hydrolases; D011133:Polysaccharide-Lyases; C016158:poly(beta-D-mannuronate) lyase