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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
biochemistry, genetics and molecular biology
Purification and characterization of a novel laccase from the ascomycete Trichoderma atroviride: Application on bioremediation of phenolic compounds
Process Biochemistry, Volume 45, No. 4, Year 2010
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Description
The extracellular laccase produced by the ascomycete Trichoderma atroviride was purified and characterized and its ability to transform phenolic compounds was determined. The purified laccase had activity towards typical substrates of laccases including 2,2′-azinobis-(3-ethylbenzthiazoline-6-sulphonate) (ABTS), dimethoxyphenol (2,6-DMP), syringaldazine and hydroquinone. The enzyme was a monomeric protein with an apparent molecular mass of 80 kDa and an isoelectric point of 3.5. The pH optima for the oxidation of ABTS and 2,6-DMP were 3 and 5, respectively, and the optimum temperature was 50 °C with 2,6-DMP. The laccase was stable at slightly acidic pH (4 and 5). It retained 80% of its activity after 4 h incubation at 40 °C. Under standard assay conditions, Km values of the enzyme were 2.5 and 1.6 mM towards ABTS and 2,6-DMP, respectively. This enzyme was able to oxidize aromatic compounds present in industrial and agricultural wastewater, as catechol and o-cresol, although the transformation of chlorinated phenols required the presence of ABTS as mediator. © 2009 Elsevier Ltd. All rights reserved.
Authors & Co-Authors
Chakroun, Hanen
Tunisia, Sfax
Centre de Biotechnologie de Sfax
Mechichi, Tahar
Tunisia, Sfax
Centre de Biotechnologie de Sfax
Martínez, María Jesús
Spain, Madrid
Csic - Centro de Investigaciones Biológicas Margarita Salas Cib
Dhouib, Abdelhafidh
Tunisia, Sfax
Centre de Biotechnologie de Sfax
Sayadi, Sami
Tunisia, Sfax
Centre de Biotechnologie de Sfax
Statistics
Citations: 116
Authors: 5
Affiliations: 2
Identifiers
Doi:
10.1016/j.procbio.2009.11.009
ISSN:
13595113