Influential parameters on the substrate selectivity of laccase and tyrosinase

Document Type : Original Article


1 Department of Chemistry, Islamic Azad University of Mashhad, Mashhad, The Islamic Republic of Iran

2 Department of Chemistry, Ferdowsi University of Mashhad, Mashhad

3 National Institute for Genetic Engineering and Biotechnology, Tehran, The Islamic Republic of Iran


Co-immobilization of several enzymes on the same matrix might enhance the efficiency of bioremediation of water resources. In pursuit of this objective, laccase and tyrosinase are especially important due to their reliance on molecular oxygen during the oxidation of various compounds. Accordingly, in this research, the substrate spectra of a laccase (obtained from Neurospora crassa) and a tyrosinase (obtained from Agaricus bisporus) were studied through analysis of their reactions with different diazo derivatives of phenol, catechol, guaiacol, and aniline, which were made from an identical molecular structure. The results were explained in view of the influential parameters on the substrate selectivity of each enzyme. The outcome of this research indicates that co-immobilization of laccase with a tyrosinase possibly expands the spectrum of the target pollutants, however, it does not guarantee the efficacy of the system against aniline derivatives.


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