Catalytic behavior and detoxifying ability of a laccase from the fungal strain Cerrena unicolor |
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| Institution: | 1. Dipartimento di Scienze Chimico-Agrarie, Università di Napoli “''Federico II”, Via Università 100, 80055 Portici, Napoli, Italy;2. Department of Biochemistry, Maria Curie-Sklodowska University, Place M. Curie-Sklodowskiej 3, PL 20 031 Lublin, Poland;1. Department of Physics, Faculty of Art and Science, Muş Alparslan University, Muş 49250, Turkey;2. Department of Science Education, Faculty of Education, Muş Alparslan University, Muş 49250, Turkey;1. Centro de Investigação em Biodiversidade e Recursos Genéticos (CIBIO), Universidade do Porto, InBIO Laboratório Associado, Campus Agrário de Vairão, 4485-661 Vairão, Portugal;2. Departamento de Biologia, Faculdade de Ciências, Universidade do Porto, R. Campo Alegre s/n, 4169-007 Porto, Portugal |
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| Abstract: | The kinetics and stability of a laccase isolated and purified from the fungal strain Cerrena unicolor were studied. The enzyme was produced in a great yield without inducers. Kinetic parameters were determined by using 2,2′-azinobis-(3-ethylbenzthiazoline-6-sulfonate) (ABTS) as substrate. At high ABTS concentrations (> 10 mM) a substrate inhibition phenomenon appeared and an inhibition constant Ki of 24 mM was determined. The pH- and temperature-profiles as well as the sensitivity of the enzyme to several deactivation agents were almost similar to those observed with laccase from different origins. Freezing-thawing treatment, high temperature, acidic pH (< 3.0) and acetonitrile strongly affected laccase activity. The laccase showed a good ability to oxidize different phenolic substances; a significant enhancing effect was showed by ABTS acting as co-substrate. These results seem to suggest that this new laccase preparation may be suitable for environmental purposes. |
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