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https://open.uns.ac.rs/handle/123456789/7665
Nаziv: | Characterization of an extracellular laccase of Leptosphaerulina chartarum | Аutоri: | Sajben-Nagy, Enikő Manczinger, László Škrbić, Biljana Živančev (Šarović), Jelena Antić, Igor Krisch, Judit Vágvölgyi, Csaba |
Ključnе rеči: | Aniline and phenol derivatives;Bioremediation;Laccase;Leptosphaerulina chartarum | Dаtum izdаvаnjа: | 1-јан-2014 | Izdаvаč: | Springer link | Čаsоpis: | World Journal of Microbiology and Biotechnology | Sažetak: | 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. © 2014 Springer Science+Business Media Dordrecht. | URI: | https://open.uns.ac.rs/handle/123456789/7665 | ISSN: | 09593993 | DOI: | 10.1007/s11274-014-1670-8 |
Nаlаzi sе u kоlеkciјаmа: | TF Publikacije/Publications |
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