A thermo-alkali-stable laccase gene from Bacillus licheniformis was cloned and expressed in Pichia pastoris. The recombinant laccase was secreted into the culture medium with a maximum activity of 227.9 U/L. The purified laccase is a monomeric glycoprotein, and its molecular weight was estimated to be 65 kDa on SDS-PAGE after deglycosylation. Optimal enzyme activity was observed at pH 6.2 and 70°C with syringaldazine as substrate. The recombinant laccase was highly stable in the pH range 7-9 after 10 days at 30°C. The enzyme displayed remarkable thermostability at 50-70°C, with a half-life of inactivation at 70°C of 6.9 h. It also exhibited high tolerance to NaCl and organic solvents like the native spore laccase. The purified laccase could rapidly decolorize reactive blue 19, reactive black 5 and indigo carmine in the presence of acetosyringone. More than 93% of the tested dyes were decolorized in 4 h at pH 9.0.
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http://dx.doi.org/10.1016/j.biortech.2013.02.015 | DOI Listing |
Environ Technol
September 2024
SAMRC Microbial Water Quality Monitoring Centre, University of Fort Hare, Alice, South Africa.
Laccase is a multicopper enzyme that plays a unique role in bioremediation of environmental pollutants. Bacteria were isolated from hospital wastewater and screened for laccase production. The laccase production process condition was optimised, and the laccase obtained was characterised.
View Article and Find Full Text PDFFront Microbiol
May 2021
Institute of Microbiology, School of Ecology and Nature Conservation, Beijing Forestry University, Beijing, China.
This study introduces a valuable laccase, designated ThLacc-S, purified from white rot fungus . ThLacc-S is a monomeric protein in nature with a molecular weight of 57.0 kDa and can efficiently metabolize endocrine disrupting chemicals.
View Article and Find Full Text PDFBioprocess Biosyst Eng
December 2020
Department of Microbiology, Panjab University, BMS Block-I, South Campus, Sector-25, Chandigarh, 160014, India.
Bioprocessing of pulp requires lignolytic as well as hemicellulolytic enzymes. The present study is the first report of a cocktail of laccase (L), xylanase (X), and mannanase (M), from a single bacterium for pulp biobleaching. A novel strain Bacillus tequilensis LXM 55 produced thermo-alkali stable L + X + M.
View Article and Find Full Text PDFIndian J Microbiol
September 2020
Department of Microbiology, BMS Block 1, South Campus, Panjab University, Chandigarh, 160014 India.
Microbial enzymes are the safe alternatives to chemical based bleaching of pulp in paper mills. For effective biobleaching, both hemicellulolytic and lignolytic enzymes are required. This study reports laccase (L) + xylanase (X) and laccase (L) + mannanase (M) enzyme concoctions for pulp biobleaching derived from sp.
View Article and Find Full Text PDFInt J Biol Macromol
October 2018
Department of Biotechnology, Chandigarh College of Technology, CGC Landran, Mohali, Punjab, 140307, India.
Decolourization of textile effluent is always being a problem of major concern for the safe disposal of effluent water in river stream. Due to intense colour of the effluent water, even after the treatment, disposal of the water in river stream is under strict environmental regulation. Laccase, a natural oxidase, have the miraculous power to decolourize different dyes with or without mediators.
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