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. 1976 Dec 1;159(3):707–713. doi: 10.1042/bj1590707

Purification and properties of an alginate lyase from a marine bacterium.

I W Davidson, I W Sutherland, C J Lawson
PMCID: PMC1164172  PMID: 1008828

Abstract

An unidentified pseudomonad isolated by enrichment procedures from decomposing seaweed was grown in defined medium containing sodium alginate as the sole carbon source. The alginate lyase recovered from disrupted bacterial cells was purified by a procedure of (NH4)2SO4 precipitation, gel filtration and ion-exchange chromatography. From sodium dodecyl sulphate/polyacrylamide-gel-electrophoresis experiments a mol.wt. of about 50 000 was determined. The enzyme was active against both 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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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