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Enzyme Research
Volume 2010, Article ID 125429, 7 pages
Research Article

Cytochrome P450 102A2 Catalyzes Efficient Oxidation of Sodium Dodecyl Sulphate: A Molecular Tool for Remediation

Laboratory of Enzyme Technology, Department of Agricultural Biotechnology, Agricultural University of Athens, Iera Odos 75, 11855 Athens, Greece

Received 5 January 2010; Revised 11 April 2010; Accepted 21 May 2010

Academic Editor: Munishwar Nath Gupta

Copyright © 2010 Irene Axarli et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Bacterial cytochrome P450s (CYPs) constitute an important family of monooxygenase enzymes that carry out essential roles in the metabolism of endogenous compounds and foreign chemicals. In the present work we report the characterization of CYP102A2 from B. subtilis with a focus on its substrate specificity. CYP102A2 is more active in oxidation of sodium dodecyl sulphate (SDS) than any other characterized CYP. The effect of SDS and NADPH concentration on reaction rate showed nonhyperbolic and hyperbolic dependence, respectively. The enzyme was found to exhibit a bell-shaped curve for plots of activity versus pH, over pH values 5.9–8.5. The rate of SDS oxidation reached the maximum value approximately at pH 7.2 and the pH transition observed controlled by two p 𝐾 a s in the acidic ( p 𝐾 a = 6 . 7 ± 0 . 0 8 ) and basic ( p 𝐾 a = 7 . 3 ± 0 . 0 6 ) pH range. The results are discussed in relation to the future biotechnology applications of CYPs.