Aryl acylamidase from Rhodococcus erythropolis NCIB 12273 |
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| Authors: | Peter A. Vaughan Geoffrey F. Hall David J. Best |
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| Affiliation: | (1) MediSense (UK) Inc., OX14 1DY Abingdon, Oxfordshire, UK;(2) Biotechnology Centre, Cranfield Institute of Technology, MK43 0AL Cranfield, Bedford, UK;(3) Present address: Biotechnology Unit, Laboratory of the Government Chemist, Queens Road, TW11 0LY Teddington, Middlesex, UK;(4) Present address: Research and Development, Sterling Organics Ltd., Edgefield Avenue, NE3 3TT Fawdon, Newcastle-Upon-Tyne, UK |
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| Abstract: | Summary A Rhodococcus erythropolis strain was isolated from soil on the basis of its ability to use acetaminophen as the sole source of both carbon and energy for growth. When grown in a complex medium containing an anilide inducer compound, the bacterium exhibited aryl acylamidase (EC 3.5.1.13) activity. This activity was not subject to carbon or nitrogen repression by the growth medium constituents as the enzyme was present throughout the exponential growth phase. The anilide was converted to the corresponding aniline, which was not further degraded. The enzyme was partially purified by a variety of methods including a batch ion exchange procedure, column ion exchange chromatography and hydrophobic interaction chromatography. The enzyme had a maximum activity at around pH 8.0 and had a Km for acetaminophen of 0.11 mM. Electrochemical assays of aryl acylamidase activity are described. The enzyme is suitable for use as a reagent in the clinical diagnostic measurement of acetaminophen.Offprint requests to: P. A. Vaughan |
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