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Catalysts 2017, 7(9), 275; doi:10.3390/catal7090275

Improving the Indigo Carmine Decolorization Ability of a Bacillus amyloliquefaciens Laccase by Site-Directed Mutagenesis

College of Life Sciences, Northeast Forestry University, Harbin 150040, China
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Received: 14 August 2017 / Revised: 29 August 2017 / Accepted: 12 September 2017 / Published: 15 September 2017
(This article belongs to the Special Issue Biocatalysis and Biotransformations)
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Abstract

Indigo carmine is a typical recalcitrant dye which is widely used in textile dyeing processes. Laccases are versatile oxidases showing strong ability to eliminate hazardous dyes from wastewater. However, most laccases require the participation of mediators for efficient decolorization of indigo carmine. Here we describe the improvement of the decolorization ability of a bacterial laccase through site-directed mutagenesis. A D501G variant of Bacillus amyloliquefaciens laccase was constructed and overexpressed in Escherichia coli. The laccase activity in the culture supernatant achieved 3374 U·L−1 for the mutant. Compared with the wild-type enzyme, the D501G exhibited better stability and catalytic efficiency. It could decolorize more than 92% of indigo carmine without additional mediators in 5 h at pH 9.0, which was 3.5 times higher than the wild-type laccase. Isatin sulfonic acid was confirmed to be the main product of indigo carmine degradation by UV-vis and LC-MS analyses. View Full-Text
Keywords: laccase; site-directed mutagenesis; extracellular expression; indigo carmine; decolorization laccase; site-directed mutagenesis; extracellular expression; indigo carmine; decolorization
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Wang, J.; Lu, L.; Feng, F. Improving the Indigo Carmine Decolorization Ability of a Bacillus amyloliquefaciens Laccase by Site-Directed Mutagenesis. Catalysts 2017, 7, 275.

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