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- Title
Production, Purification, and Characterization of Recombinant Bhargavaea beijingensis Laccase for Potential Lignin Degradation and Dyes Decolorization.
- Authors
Chaudhary, Sonal; Varma, Ajit; Jha, Saurabh; Patel, Sanjay K. S.; Porwal, Shalini
- Abstract
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 °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 μmol/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.
- Subjects
LACCASE; LIGNINS; CONGO red (Staining dye); AFFINITY chromatography; COPPER ions; METAL ions; CATALYTIC activity
- Publication
Catalysis Letters, 2024, Vol 154, Issue 4, p1537
- ISSN
1011-372X
- Publication type
Article
- DOI
10.1007/s10562-023-04394-z