Abstract
Laccase-producing fungi were isolated from air, using selective media with a chromogenic substrate to indicate enzyme activity. The best laccase producer strain proved to be a Leptosphaerulina chartarum isolate. Laccase production was investigated in the presence of various inducers in different cultivation conditions. The extracellular laccase was purified for further investigations. SDS-PAGE showed that this laccase is a monomeric protein of 38 kDa molecular weight. The enzyme is active in the pH-range of 3.5–6, with an optimum at pH 3.8. It is active in the 10–60 °C temperature range, with an optimum at 40 °C. After 20 min incubation at temperatures above 70 °C the enzyme lost its activity. Degradation of seven aniline and phenol compounds (2,4-dichlorophenol; 2-methyl-4-chlorophenol; 3-chloroaniline; 4-chloroaniline; 2,6-dimethylaniline; 3,4-dichloroaniline and 3-chloro-4-methylaniline) was investigated, with or without guaiacol (2-methoxyphenol) as mediator molecule. Addition of a mediator to the system significantly increased the degradation levels. These results confirmed that the isolated laccase is able to convert these harmful xenobiotics at in vitro conditions.
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Acknowledgments
This study was supported by the project LACREMED (HU-SRB 1002/214/147) co-financed by the European Union through the Hungary-Serbia IPA Cross-border Co-operation Programme and also supported by Ministry of Education, Science and Technological Development of the Republic of Serbia (Project No. 172050).
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Sajben-Nagy, E., Manczinger, L., Škrbić, B. et al. Characterization of an extracellular laccase of Leptosphaerulina chartarum . World J Microbiol Biotechnol 30, 2449–2458 (2014). https://doi.org/10.1007/s11274-014-1670-8
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DOI: https://doi.org/10.1007/s11274-014-1670-8