Purification and properties of an alginate lyase from a marine bacterium

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Abstract
An unidentified pseudomonad isolated by enrichment procedures from decomposing seaweed was grown in defined medium containing sodium alginate as the sole C source. The alginate lyase [EC 4.2.2.3] recovered from disrupted bacterial cells was purified by a procedure of (NH4)2SO4 precipitation, gel filtration and ion-exchange chromatography. From sodium dodecyl sulfate/polyacrylamide-gel-electrophoresis experiments, a MW of .apprx. 50,000 was determined. The enzyme was active against algal and bacterial alginate preparations. Kinetic studies together with analysis of the unsaturated oligouronide products of alginate lyase action indicated the enzyme was specific for guluronic acid-containing regions of the macromolecular substrate. The specificity of the enzyme can be used to give information about the primary composition of alginate samples.