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Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a

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2016
Expression_and_characterization_acc_2016.pdf (904.4Kb)
Authors
Lončar, Nikola L.
Božić, Nataša
Vujčić, Zoran
Article (Accepted Version)
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Abstract
Bacterial laccases have proven advantages over fungal and plant counterparts in terms of wider pH optimum, higher stability and broader biocatalytic scope. In this work, Bacillus licheniformis ATCC 9945a laccase is produced heterologously in Escherichia coli. Produced laccase exhibits remarkably high temperature optimum at 90 degrees C and possess significant thermostability and resistance to inactivation by organic solvents. Laccase has an apparent melting temperature of 79 degrees C at pH 7.0 and above 70 degrees C in range of pH 5.0-8.0, while having half-life of 50 min at 70 degrees C. Presence of 10% organic solvents such as acetonitrile, dimethylformamide, dimethylsulfoxide or methanol reduces melting temperature to 45-52 degrees C but activity remains practically unimpaired. With 50% of acetonitrile and methanol laccase retained similar to 40% of initial activity. EDTA and 300 mM sodium -chloride have positive effect on activity. Enzyme is active on syringaldazine, ABTS, phenols..., amines, naphthol, lignin and lignin model compounds and mediates C-C bond formation via oxidative coupling after one electron oxidation of phenolic group. Successful polymerization of 2 -naphthol was achieved with 77% conversion of 250 mg/L 2-naphtol in only 15 min which may further expand substrate scope of this enzyme towards polymer production and/or xenobiotics removal for environmental applications. (C) 2016 Elsevier B.V. All rights reserved.

Keywords:
Laccase / Bacillus licheniformis / Oxidation / Thermostable enzyme / Lignin
Source:
Journal of Molecular Catalysis. B: Enzymatic, 2016, 134, 390-395
Publisher:
  • Elsevier Science Bv, Amsterdam
Funding / projects:
  • Production, purification and characterization of enzymes and small molecules and their application as soluble or immobilized in food biotechnology, biofuels production and environmental protection (RS-172048)
Note:
  • This is peer-reviewed version of the following article: Loncar, N.; Bozic, N.; Vujcic, Z. Expression and Characterization of a Thermostable Organic Solvent-Tolerant Laccase from Bacillus Licheniformis ATCC 9945a. J. Mol. Catal. B-Enzym. 2016, 134, 390–395. https://doi.org/10.1016/j.molcatb.2016.06.005
  • Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3518

DOI: 10.1016/j.molcatb.2016.06.005

ISSN: 1381-1177

WoS: 000391074700017

Scopus: 2-s2.0-85003014042
[ Google Scholar ]
22
12
URI
https://cherry.chem.bg.ac.rs/handle/123456789/3517
Collections
  • Publikacije / Publications
  • Publikacije / Publications
Institution/Community
Hemijski fakultet / Faculty of Chemistry
TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3517
AB  - Bacterial laccases have proven advantages over fungal and plant counterparts in terms of wider pH optimum, higher stability and broader biocatalytic scope. In this work, Bacillus licheniformis ATCC 9945a laccase is produced heterologously in Escherichia coli. Produced laccase exhibits remarkably high temperature optimum at 90 degrees C and possess significant thermostability and resistance to inactivation by organic solvents. Laccase has an apparent melting temperature of 79 degrees C at pH 7.0 and above 70 degrees C in range of pH 5.0-8.0, while having half-life of 50 min at 70 degrees C. Presence of 10% organic solvents such as acetonitrile, dimethylformamide, dimethylsulfoxide or methanol reduces melting temperature to 45-52 degrees C but activity remains practically unimpaired. With 50% of acetonitrile and methanol laccase retained similar to 40% of initial activity. EDTA and 300 mM sodium -chloride have positive effect on activity. Enzyme is active on syringaldazine, ABTS, phenols, amines, naphthol, lignin and lignin model compounds and mediates C-C bond formation via oxidative coupling after one electron oxidation of phenolic group. Successful polymerization of 2 -naphthol was achieved with 77% conversion of 250 mg/L 2-naphtol in only 15 min which may further expand substrate scope of this enzyme towards polymer production and/or xenobiotics removal for environmental applications. (C) 2016 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Molecular Catalysis. B: Enzymatic
T1  - Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a
VL  - 134
SP  - 390
EP  - 395
DO  - 10.1016/j.molcatb.2016.06.005
ER  - 
@article{
author = "Lončar, Nikola L. and Božić, Nataša and Vujčić, Zoran",
year = "2016",
abstract = "Bacterial laccases have proven advantages over fungal and plant counterparts in terms of wider pH optimum, higher stability and broader biocatalytic scope. In this work, Bacillus licheniformis ATCC 9945a laccase is produced heterologously in Escherichia coli. Produced laccase exhibits remarkably high temperature optimum at 90 degrees C and possess significant thermostability and resistance to inactivation by organic solvents. Laccase has an apparent melting temperature of 79 degrees C at pH 7.0 and above 70 degrees C in range of pH 5.0-8.0, while having half-life of 50 min at 70 degrees C. Presence of 10% organic solvents such as acetonitrile, dimethylformamide, dimethylsulfoxide or methanol reduces melting temperature to 45-52 degrees C but activity remains practically unimpaired. With 50% of acetonitrile and methanol laccase retained similar to 40% of initial activity. EDTA and 300 mM sodium -chloride have positive effect on activity. Enzyme is active on syringaldazine, ABTS, phenols, amines, naphthol, lignin and lignin model compounds and mediates C-C bond formation via oxidative coupling after one electron oxidation of phenolic group. Successful polymerization of 2 -naphthol was achieved with 77% conversion of 250 mg/L 2-naphtol in only 15 min which may further expand substrate scope of this enzyme towards polymer production and/or xenobiotics removal for environmental applications. (C) 2016 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Molecular Catalysis. B: Enzymatic",
title = "Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a",
volume = "134",
pages = "390-395",
doi = "10.1016/j.molcatb.2016.06.005"
}
Lončar, N. L., Božić, N.,& Vujčić, Z.. (2016). Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a. in Journal of Molecular Catalysis. B: Enzymatic
Elsevier Science Bv, Amsterdam., 134, 390-395.
https://doi.org/10.1016/j.molcatb.2016.06.005
Lončar NL, Božić N, Vujčić Z. Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a. in Journal of Molecular Catalysis. B: Enzymatic. 2016;134:390-395.
doi:10.1016/j.molcatb.2016.06.005 .
Lončar, Nikola L., Božić, Nataša, Vujčić, Zoran, "Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a" in Journal of Molecular Catalysis. B: Enzymatic, 134 (2016):390-395,
https://doi.org/10.1016/j.molcatb.2016.06.005 . .

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