Purification, characterization, and cloning of an extracellular laccase with potent dye decolorizing ability from white rot fungus Cerrena unicolor GSM-01

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• 作者：Shan-Shan Wang^a ; ^b ; Ying-Jie Ning^a ; Shou-Nan Wang^a ; Jing Zhang^a ; Guo-Qing Zhang^a ; ^{zhanggqbua@163.com} ; Qing-Jun Chen^b ; ^{cqj3305@126.com}
• 关键词：Laccase ; Cerrena unicolor ; Purification and cloning
• 刊名：International Journal of Biological Macromolecules
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：95
• 期：Complete
• 页码：920-927
• 全文大小：2951 K
• 卷排序：95

文摘

A novel laccase was purified from fermentation broth of the white rot fungus Cerrena unicolor strain GSM-01 following three ion-exchange chromatography steps and one gel-filtration step. The purified enzyme was determined to be a monomeric protein of 63.2 kDa and demonstrated high oxidation activity of 2.05 × 104 U/mg towards ABTS. Its cDNA, gene, and amino acid sequences were obtained. It possessed high sequence similarity with that of other laccases but different enzymatic properties. It manifested optimal pH and temperature of 2.6 and 45 °C, respectively. Fe3+ and Fe2+ were the most efficient inhibitors towards Cerrena unicolor laccase (CUL), while Mn2+ can slightly enhance the laccase activity of 3.8–10.5%. The Km and Vmax of CUL were estimated to 302.7 μM and 13.6 μM m−1, respectively. CUL was effective in the decolorization of bromothymol blue, evans blue, methyl orange, and malachite green with decolorization efficiencies of 50%–85%. It possesses potential application in textile and environmental industries.