Studies on Laccase Activity in the Filamentous Fungus Trichoderma reesei

Laccase have been mainly studied in wood rot fungal species of the basidiomycetes family especially in white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccase activity from Trichoderma reesei in catechol based medium. Results showed that laccase enzyme from T.reesei was active in acidic pH range and that optimum pH was 4.5. The optimum temperature of laccase from T. reesei was also 27 0 C. Laccase activity in medium containing 10 gL -1 catechol was 1.22 U ml -1 , which was more than 6 times higher than in medium containing 10 gL -1 glucose. Laccase activity of T.reesei was also determined in different catechol concentrations. At a concentration of 15 gL -1 , laccase activity slightly decreased and the obtained maximum activity was 1.1 Uml -1 . Laccase activity of T. reesei was found higher than glucose, in the medium containing catechol as carbon source. Laccase have been mainly studied in wood rot fungal species of the basidiomycetes family especially in white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccase activity from Trichoderma reesei in catechol based medium. Results showed that laccase enzyme from T.reesei was active in acidic pH range and that optimum pH was 4.5. The optimum temperature of laccase from T. reesei was also 27 0 C. Laccase activity in medium containing 10 gL -1 catechol was 1.22 U ml -1 , which was more than 6 times higher than in medium containing 10 gL -1 glucose. Laccase activity of T.reesei was also determined in different catechol concentrations. At a concentration of 15 gL -1 , laccase activity slightly decreased and the obtained maximum activity was 1.1 Uml -1 . Laccase activity of T. reesei was found higher than glucose, in the medium containing catechol as carbon source. Laccase have been mainly studied in wood rot fungal species of the basidiomycetes family especially in white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccase activity from Trichoderma reesei in catechol based medium. Results showed that laccase enzyme from T.reesei was active in acidic pH range and that optimum pH was 4.5. The optimum temperature of laccase from T. reesei was also 27 0 C. Laccase activity in medium containing 10 gL -1 catechol was 1.22 U ml -1 , which was more than 6 times higher than in medium containing 10 gL -1 glucose. Laccase activity of T.reesei was also determined in different catechol concentrations. At a concentration of 15 gL -1 , laccase activity slightly decreased and the obtained maximum activity was 1.1 Uml -1 . Laccase activity of T. reesei was found higher than glucose, in the medium containing catechol as carbon source. Laccase have been mainly studied in wood rot fungal species of the basidiomycetes family especially in white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccase activity from Trichoderma reesei in catechol based medium. Results showed that laccase enzyme from T.reesei was active in acidic pH range and that optimum pH was 4.5. The optimum temperature of laccase from T. reesei was also 27 0 C. Laccase activity in medium containing 10 gL -1 catechol was 1.22 U ml -1 , which was more than 6 times higher than in medium containing 10 gL -1 glucose. Laccase activity of T.reesei was also determined in different catechol concentrations. At a concentration of 15 gL -1 , laccase activity slightly decreased and the obtained maximum activity was 1.1 Uml -1 . Laccase activity of T. reesei was found higher than glucose, in the medium containing catechol as carbon source.