Laccase enzymes are polyphenol oxidase that catalyze the oxidation of wide range of phenolic components including phenols, polyphenols, aromatic amines and non-phenolic substitution with molecular oxygen as electron acceptor. So these enzymes have biotechnological application such as wastewater treatment system, bioremediation of soil pollution and etc. Result from previous studies showed an increase in thermal stability of bacterial laccase from Bacillus sp. HR03 using site directed mutagenesis and the effect of E188 residue on the surface regions at the interface between domain 1 and 2 in stability was confirmed. The aim of the present work was to investigate the effect of this amino acid substitution on enzyme activity in the presence of dimethyl sulfoxide and dimethylformamide as organic solvents. Compression of kinetic parameters including Kcat / Km ، ∆∆G‡, C50 showed significant increases in the mutant enzyme than wild type enzyme, that industrial application of the enzyme will be easy.

Keywords: Laccase enzyme, site-directed mutagenesis, Solvent stability

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