Abstract
Laccase activity was detected in a soil bacterium Stenotrophomonas maltophilia AAP56 identified by biochemical and molecular methods. It was produced in cells at the stationary growth phase in Luria Bertani (LB) medium added by 0.4 mM copper sulfate. The addition of CuSO4 in culture medium improved production of laccase activity. However, one laccase enzyme was detected by native polyacrylamide gel electrophoresis. The enzyme showed syringaldazine (K m = 53 μM), 2,2’-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (K m = 700 μM), and pyrocatechol (K m = 25 μM) oxidase activity and was activated by addition of 0.1% (v/v) Triton-X-100 in the reaction mixture. Moreover, the laccase activity was increased 2.6-fold by the addition of 10 mM copper sulfate; the enzyme was totally inhibited by ethylenediaminetetraacetic acid (5 mM), suggesting that this laccase is a metal-dependant one. Decolorization activity of some synthetic dyes (methylene blue, methyl green, toluidine blue, Congo red, methyl orange, and pink) and the industrial effluent (SITEX Black) was achieved by the bacteria S. maltophilia AAP56 in the LB growth medium under shaking conditions.
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Acknowledgements
The authors gratefully thank Dr Ali Amor (Laboratoire d’analyses biomédicales, Hopital Militaire) for Api identification and Pr. Ali Gargouri from CBS Sfax for DNA sequencing. This work was supported by the Tunisian Ministry of Higher Education, Scientific Research, and Technology (Financial project of Bioengineering Unit 99 UR/09-26).
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Galai, S., Limam, F. & Marzouki, M.N. A New Stenotrophomonas maltophilia Strain Producing Laccase. Use in Decolorization of Synthetics Dyes. Appl Biochem Biotechnol 158, 416–431 (2009). https://doi.org/10.1007/s12010-008-8369-y
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DOI: https://doi.org/10.1007/s12010-008-8369-y