Primary Alcohol Sulfatase in a Pseudomonas Species

Abstract

An ammonium sulfate-precipitated fraction from cell-free extracts of Pseudomonas C12B grown on a medium containing sodium dodecyl sulfate (SDS) contained alkyl sulfatase increased fourfold in specific activity over the crude. Optimal p H (7.5) and temperature (70 C) for sulfate release were determined with SDS labeled with radioactive sulfur (SDS 35 ) as test substrate. Phosphate, arsenate, and certain heavy metal ions inhibited desulfation, whereas Mg ++ and Mn ++ stimulated activity of preparations which had been dialyzed against ethylenediaminetetraacetic acid. Dodecanol was recovered in semiquantitative yield from reaction mixtures containing enzyme and SDS 35 . Aryl sulfates, secondary alcohol sulfates, and a phenoxyethyl sulfate failed to serve as substrate for this enzyme.