Abstract
This review gives an overview on the occurrence of sulfatases in Prokaryota, Eukaryota and Archaea. The mechanism of enzymes acting with retention or inversion of configuration during sulfate ester hydrolysis is discussed taking two complementary examples. Methods for the discovery of novel alkyl sulfatases are described by way of sequence-based search and enzyme induction. A comprehensive list of organisms with their respective substrate scope regarding prim- and sec-alkyl sulfate esters allows to assess the capabilities and limitations of various biocatalysts employed as whole cell systems or as purified enzymes with respect to their activities and enantioselectivities. Methods for immobilization and selectivity enhancement by addition of metal ions or organic (co)solvents are summarised.
Highlights
This review gives an overview on the occurrence of sulfatases in Prokaryota, Eukaryota and Archaea
The enzymatic ring opening of oxiranes is achieved by epoxide hydrolases (EC 3.3.2.3), which serves as detoxification strategy to yield more innocuous diols (Kotik et al 2012)
(Wallner et al 2005b) n.a. not applicable, n.d. not determined a In kinetic resolutions showing high enantioselectivity, the maximum conversion is 50 % b Enantioselectivity is expressed as the ratio of the reaction rate of enantiomers ('enantiomeric ratio', E) (Straathof and Jongejan 1997) c Unpublished results d Improved E values in presence of organic cosolvents e Crude enzyme preparation alkyl sulfatase activity (Hallmann and Sumper 1994; Selmer et al 1996)
Summary
This review gives an overview on the occurrence of sulfatases in Prokaryota, Eukaryota and Archaea. A zymographic analysis of Pseudomonas strain AE-A showed up to three different alkyl sulfatases, depending on the nature of the supplemented sulfur source.
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