Purification and characteristics of an alginase from Alginovibrio aquatilis.
An exocellular inducible alginase from a strain of Alginovibrio aquatilis was purified 61-fold by ammonium sulfate precipitation and column chromatography on Sephadex G-150 and diethylaminoethyl-cellulose. The purified enzyme was more resistant than the crude enzyme to elevated temperatures. The monovalent cations Cs+, Rb+, K+, Na+, and Li+, in order of decreasing enzyme activation, were required for activity. The pH optimum of the purified alginase was 8.0 and its molecular weight from exclusion chromatography on Sephadex G-150 was 110,000.
D000464:Alginates / Q000378:metabolism; D001419:Bacteria / Q000201:enzymology* / Q000378:metabolism; D002414:Cations, Monovalent; D006026:Glycoside Hydrolases / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D012623:Seawater; D014871:Water Microbiology
D000464:Alginates; D002414:Cations, Monovalent; D006026:Glycoside Hydrolases