Laccase of the lignolytic fungus Trametes hirsuta: Purification and characterization of the enzyme, and cloning and primary structure of the gene

The Trametes hirsuta 072 laccase multigene family: Genes identification and transcriptional analysis under copper ions induction

“…It should be underlined that only 4 and 2 different laccase isozymes have been isolated and characterized from T. versicolor and T. cinnabarina respectively [39,49,51,52]. At the beginning of our study, only one gene encoding laccase in T. hirsuta 072, was known [53].…”

Fungal proteinaceous compounds with multiple biological activities

“…Detailed structural information and in some cases structurefunction relationships is (are) available for some of the fungal lectins (Lyimo et al, 2011), laccases (Piontek et al, 2002;Rebrikov et al, 2006;Ferraroni et al, 2014), ribosomeinactivating proteins (Sacco et al, 1983;López-Otín et al, 1984;Martínez del Pozo et al, 1988;Gasset et al, 1995., Kao and Davies, 1999, 2000Pérez-Cañadillas et al, 2000;García-Mayoral et al, 2005;Alvarez-García et al, 2006), and nucleases Kobayashi et al, 2000Kobayashi et al, , 2003Kobayashi et al, , 2014.…”

Laccase-aided protein modification: Effects on the structural properties of acidified sodium caseinate gels

“…1a and b, lanes 5 and 6). At 45 C, which is close to optimum temperature of T. hirsuta laccase (Rebrikov et al, 2006;Shleev et al, 2004), the reaction was much faster and higher extent of protein polymerization could be observed compared with when the reaction was carried out at room temperature. Treatment of sodium caseinate with laccase A resulted in formation of polymerization products, but also formation of low molecular weight protein bands was clearly observed with both enzyme dosages.…”