Basidiomycetes sınıfında bulunan beyaz çürükçül mantarlar en çok çalışılmış lakkaz üreten mantarlardır. Diğer mantar ailelerinde lakkaz enzimi ile ilgili araştırmalar büyük ölçüde eksiktir. Bu çalışmada, Trichoderma reesei küf mantarında ve kateşol içeren ortamda lakkaz aktivitesi incelendi. Deneysel çalışmadan elde edilen sonuçlara göre, Trichoderma reesei’de lakkaz enziminin asidik pH’da aktif olduğu gözlendi. Lakkaz enziminin optimum pH’sı 4.5 olarak belirlendi. Trichoderma reesei’de lakkaz enziminin optimum sıcaklığı da 27ºC’olarak tespit edildi. 10 gL kateşol içeren ortamda, Trichoderma reesei’de lakkaz enziminin aktivitesi 10gL glukoz içeren ortam’a göre 6 kat daha fazla bulundu. Lakkaz aktivitesi 1,22 U ml olarak belirlendi. Trichoderma reesei’de lakkaz aktivitesi farklı kateşol konsantrasyonları için de tespit edildi. 15gL kateşol konsantrasyonunda lakkaz aktivitesinin azaldığı gözlendi. 15gL kateşol konsantrasyonunda maksimum lakkaz aktivitesi 1,1 UmL olarak belirlendi.

Laccase have been mainly studied in wood rot fungal species of the basidiomycetes family especiallyin white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccaseactivity fromTrichoderma 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 oflaccase from T. reesei was also 270C. Laccase activity in medium containing 10 gL-1 catechol was 1.22U ml  -1, which was more than 6 times higher than in medium containing 10 gL-1 glucose. Laccase activityof  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 activityof  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 especiallyin white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccaseactivity fromTrichoderma 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 oflaccase from T. reesei was also 270C. Laccase activity in medium containing 10 gL-1 catechol was 1.22U ml  -1, which was more than 6 times higher than in medium containing 10 gL-1 glucose. Laccase activityof  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 activityof  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 especiallyin white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccaseactivity fromTrichoderma 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 oflaccase from T. reesei was also 270C. Laccase activity in medium containing 10 gL-1 catechol was 1.22U ml  -1, which was more than 6 times higher than in medium containing 10 gL-1 glucose. Laccase activityof  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 activityof  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 especiallyin white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccaseactivity fromTrichoderma 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 oflaccase from T. reesei was also 270C. Laccase activity in medium containing 10 gL-1 catechol was 1.22U ml  -1, which was more than 6 times higher than in medium containing 10 gL-1 glucose. Laccase activityof  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 activityof  T. reesei was found higher than glucose, in the medium containing catechol as carbon source.