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   <subfield code="a">Biodegradation of short-chain alkyl sulphates by a coryneform species</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Graham White, Paul Matts]</subfield>
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   <subfield code="a">Coryneform B1a isolated from soil grew well on butyl-, pentyl- and hexyl-1-sulphates esters and on the corresponding parent alcohols as sole sources of carbon, with growth rates around 0.14-0.19 h-1. Propyl-1-sulphate and heptyl-1-sulphate supported slower growth, and their C1, C2 and C8 homologues were not utilised at all. Growth of the organism was accompanied by disappearance of butyl-1-sulphate. In the presence of resting cells, butyl-1-sulphate degradation was stoichiometric with the liberation of inorganic sulphate. Butan-1-ol was also detected but in less than stoichiometric amounts. Non-denaturing polyacrylamide gel electrophoresis of extracts of cells grown on butyl-1-sulphate, followed by incubation of gels in butyl-1-sulphate and precipitation of liberated SO4 2- as BaSO4, revealed a single white band of alkylsulphatase activity. Other zymograms produced in the same way but incubated with the C5 and C6 esters, each produced a single band of the same mobility and intensity. With the C3 and C7 homologues, the same band was present but considerably less intense. No alkylsulphatase band was detected for methyl, ethyl or octyl-1-sulphates. Assays of alkylsulphatase activity in crude cell-extracts indicated maximum activity towards butyl-1-sulphate at pH 7.5 and 30° C, with Km=8.4±1.4 mM and V max =0.13±0.01 μmol/min/mg of protein. The results indicated that degradation of short-chain alkyl sulphates in this organism was initiated by enzymic hydrolysis to the corresponding alcohol.</subfield>
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   <subfield code="a">alkylsulphatase</subfield>
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