en Related Fields Related Fields مقاله کامل Full Length/Original Article <strong>Background</strong>: Phenolic compounds, which are produced routinely by industrial and urban activities, possess dangers to live organisms and environment. Laccases are oxidoreductase enzymes with the ability of remediating a wide variety of phenolic compounds to more benign molecules. The purpose of the present research is surface display of a laccase enzyme with adhesin involved in diffuse adhesion (AIDA-I) autotransporter system on the surface of <em>Escherichia coli</em> cells for bioremediation of phenolic compounds. <strong>Methods</strong>: The expression of laccase was regulated by a phenol-responsive promoter (a &sigma;⁵⁴ promoter). The constitutively-expressed CapR transcription activator was able to induce laccase expression in the presence of phenolic compounds. <strong>Results</strong>: Western blot analysis showed the expression and correct transfer of the enzyme to the outer membrane of <em>E. coli</em> cells in the presence of phenol. Activity assay confirmed the correct folding of the enzyme after translocation through the autotransporter system. HPLC analysis of residual phenol in culture medium showed a significant reduction of phenol concentration in the presence of cells displaying laccase on the surface. <strong>Conclusion</strong>: Our findings confirm that autodisplay enables functional surface display of laccase for direct substrate-enzyme availability by overcoming membrane hindrance. Laccase, Phenol, Bioremediation, AIDA-I 202 209 http://ibj.pasteur.ac.ir/browse.php?a_code=A-10-1-701&slc_lang=en&sid=1 Mehrnoosh Fathi-Roudsari Yes National Institute of Genetic Engineering and Biotechnology, Tehran, Iran Mehrdad Behmanesh No Department of Genetics, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran Ali-Hatef Salmanian No National Institute of Genetic Engineering and Biotechnology, Tehran, Iran Majid Sadeghizadeh No Department of Genetics, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran Khosro Khajeh No Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran