Purification, characterization and decolourization ability of Fomes fomentarius laccase produced in solid medium

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• 作者：Mohamed Neifar ; Atef Jaouani ; Raoudha Ellouze-Ghorbel ; Semia Ellouze-Chaabouni
• 关键词：Laccase ; Fomes fomentarius ; Phenols oxidation ; Remazol Brilliant Blue R decolourization
• 刊名：Journal of Molecular Catalysis B: Enzymatic
• 出版年：2010
• 出版时间：June 2010
• 年：2010
• 卷：64
• 期：1-2
• 页码：68-74
• 全文大小：498 K

文摘

Laccase produced by Fomes fomentarius grown on wheat bran in solid cultures was purified to electrophoretic homogeneity by ammonium sulfate precipitation, size-exclusion chromatography and anion-exchange chromatography. A single laccase was found having apparent molecular mass of 51 kDa. The N-terminal amino acid sequence was IGPKTDLTIATGDVSPDG and the highest similarity value was found to the laccase from Trametes sp. 420 (94 % ). The enzyme exhibits a temperature optimum of 60 °C and has a half-life of 66 min at 60 °C. It manifested maximal activity at pH 4 and showed K_m, k_cat and k_cat/K_m values of 26 μM, 106 s⁻¹ and 4 × 10⁶ s⁻¹ M⁻¹, respectively, with 2,6-dimethoxyphenol as substrate. The purified laccase was resistant to several metal ions such as Cd²⁺, Fe²⁺, Zn²⁺, Mg²⁺, Mn²⁺ and Cu²⁺. In addition, the enzyme had ability to decolourize the anthraquinone dye Remazol Brilliant Blue R without mediators.