Production, Purification, and Characterization of Recombinant Bhargavaea beijingensis Laccase for Potential Lignin Degradation and Dyes Decolorization

Bacterial laccase has grown significantly crucial on a large scale because they have high catalytic activity and stability. This is the first study in which the laccase gene was amplified from Bhargavaea beijingensis, ligated to the pENTR-TOPO vector, and transformed into Escherichia coli. The novel laccase was purified by Ni-NTA sepharose affinity chromatography. Purified laccase showed optimum pH and temperature of 8.0 and 50 degrees C, respectively. The novel B. beijingensis laccase exhibited stable activity at a broad range of pH and temperature. The kinetic parameters Km of 0.23 mM and Vmax of 54.6 mu mol/min/ mg of protein were noted for recombinant laccase toward guaiacol. Laccase activity was significantly influenced by metal ions such as copper, magnesium, and arsenate. The efficacy of laccase in dye decolorization was investigated using various dyes, and a nearly complete decolorization of congo red was recorded. This study confirmed that laccase from B. beijingensis can be produced in the active and stable form to degrade lignin and decolorize dyes. [GRAPHICS]

Automated summary

Bacterial laccase from Bhargavaea beijingensis was successfully amplified, transformed, and purified. The purified laccase showed optimum pH and temperature at 8.0 and 50 degrees C, respectively, and exhibited stable activity across a broad range of pH and temperature. The laccase demonstrated significant dye decolorization capability, particularly towards congo red.