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Appl Environ Microbiol. 1977 May; 33(5): 1156-1161

Purification and characteristics of an alginase from Alginovibrio aquatilis.

R A Stevens and R E Levin

ABSTRACT

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.

Appl Environ Microbiol. 1977 May; 33(5): 1156-1161






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