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Trametes versicolor, laccase

Figure 17.3 Anatomy of a redox enzyme representation of the X-ray crystallographic structure of Trametes versicolor laccase III (PDB file IKYA) [Bertrand et al., 2002]. The protein is represented in green lines and the Cu atoms are shown as gold spheres. Sugar moieties attached to the surface of the protein are shown in red. A molecule of 2,5-xyhdine that co-crystallized with the protein (shown in stick form in elemental colors) is thought to occupy the broad-specificity hydrophobic binding pocket where organic substrates ate oxidized by the enzyme. Electrons from substrate oxidation are passed to the mononuclear blue Cu center and then to the trinuclear Cu active site where O2 is reduced to H2O. (See color insert.)... Figure 17.3 Anatomy of a redox enzyme representation of the X-ray crystallographic structure of Trametes versicolor laccase III (PDB file IKYA) [Bertrand et al., 2002]. The protein is represented in green lines and the Cu atoms are shown as gold spheres. Sugar moieties attached to the surface of the protein are shown in red. A molecule of 2,5-xyhdine that co-crystallized with the protein (shown in stick form in elemental colors) is thought to occupy the broad-specificity hydrophobic binding pocket where organic substrates ate oxidized by the enzyme. Electrons from substrate oxidation are passed to the mononuclear blue Cu center and then to the trinuclear Cu active site where O2 is reduced to H2O. (See color insert.)...
Trametes versicolor laccase Glutaraldehyde crosslinking to pH = 6.0, aeration of cell 0.45 0.06 [130] ... [Pg.247]

A systematic approach using Trametes versicolor laccase co-immobilized with osmium-based redox polymers has highlighted the importance of redox complex loading [144, 145], and of the redox potential of the redox polymer [22], on ORR current density. Increasing ORR current density is observed with increased difference in redox potential between the Tl site of laccase and redox polymer, but maximum power from an EFC is predicted to result using a redox polymer of redox potential 0.17 V more negative than the Tl site of laccase. It would be inter-... [Pg.254]

R Bourbonnais, MG Paice. Demethylation and delignification of kraft pulp by Trametes versicolor laccase in the presence of 2,2 azinobis-(3-ethylbenzthiazoline-6-sulphonate). [Pg.519]

Trametes versicolor laccase Kaolinite Oxidation of anthracene [49]... [Pg.39]

Trametes versicolor laccase Calcareous clay soil Atrazine bioremediation [50]... [Pg.39]

Trametes versicolor laccase Graphite Biosensors for phenolic compounds [81]... [Pg.43]

Trametes versicolor laccase Carbon nanotubes -ionic liquid gel on graphite Electrode for direct electrocatalytic reduction of 02 to H20 [83]... [Pg.43]

Trametes versicolor laccase MWCNT/chitosan Oxygen biosensor, biofuel cells [121]... [Pg.48]

Bohlin C, Jonsson LJ, Roth R, van Zyl WH. Heterologous expression of Trametes versicolor laccase in Pichia pastoris and Aspergillus niger. Appl Biochem Biotechnol 2006 129(1-3) 195-214. [Pg.32]

Tortolini C, Rea S, Carota E, Cannistraro S, Mazzei F. Influence of the immobilization procedures on the electroanalytical performances of Trametes versicolor laccase based bioelectrode. Microchem J 2012 100 8-13. [Pg.220]


See other pages where Trametes versicolor, laccase is mentioned: [Pg.716]    [Pg.428]    [Pg.743]    [Pg.252]    [Pg.253]    [Pg.258]    [Pg.147]    [Pg.147]    [Pg.405]    [Pg.194]    [Pg.405]    [Pg.3965]    [Pg.11]    [Pg.18]    [Pg.86]    [Pg.210]    [Pg.242]   
See also in sourсe #XX -- [ Pg.39 , Pg.43 , Pg.48 , Pg.204 ]

See also in sourсe #XX -- [ Pg.194 , Pg.241 , Pg.243 ]

See also in sourсe #XX -- [ Pg.11 ]




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Laccases

Laccases from Trametes versicolor

Trametes versicolor

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