Kinetic studies on the reaction between Trametes villosa laccase and dioxygen

Heterologous laccase production and its role in industrial applications

“…Likewise, the recombinant laccase of Trametes villosa in A. oryzae was investigated to elucidate the reaction mechanism of the reduction of dioxygen to water by stopped-flow experiments and under steady-state conditions. 134 Moreover, the availability of high yields of recombinant proteins has allowed solving 3D structures of the laccase from Coprinus cinereus 139 and bacterial laccase from S. coelicolor expressed in A. oryzae, 144 and that from M. albomyces expressed in T. reesei.…”

Oxidative coupling of various aromatic phenols and anilines in water using a laccase from Trametes villosa and insights into the ‘PEG effect’

“…27 PEI, the only cationic polymer used, had a deleterious effect and it is thought that it may interact with the enzyme itself due to its supposed negative charge (the pI for laccase in this study was not measured, but the white rot fungal enzyme pIs are in the range 3.5-4.2. 40,42 It has been suggested that the additives' polymeric structure and interaction with the enzyme may both be contributing factors to the observed additive effect, particularly with laccases having pI above 5.5. 27,42 This observation, based on kinetic data, could also be explained if less enzyme was inactivated during the initial stages of the reaction due to additive-product/intermediate interactions.…”

Kinetic modeling of a bi‐enzymatic system for efficient conversion of lactose to lactobionic acid

“…Even though a laccase originating from the Japanese lacquer tree Rhus vernicifera was the subject of study (Petersen and Degn, 1978), the results of this study can be extended to fungal laccases (Kurniawati and Nicell, 2005) as proven for the LAC originating from Trametes villosa (Bukh et al, 2006). As ABTS is a one-electron donor (the ABTS dication is not formed by laccase), four molecules of ABTS are oxidized per molecule of oxygen reduced to water.…”