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Laccases

The reactions catalyzed by laccases proceed by the monoelectronic oxidation of a suitable substrate molecule (phenols and aromatic or aliphatic amines) to the corresponding reactive radical (Riva, 2006). The redox process takes place with the assistance of a cluster of four copper atoms that form the catalytic core of the enzyme they also confer the typical blue color to these enzymes because of the intense electronic absorption of the Cu-Cu linkages (Piontek et al., 2002). The overall outcome of the catalytic cycle is the reduction of one molecule of oxygen to two molecules of water and the concomitant oxidation of four substrate molecules to produce four [Pg.7]

Research on Enzymes in the Pulp and Paper Industry 6.3.4.1 Laccases [Pg.150]

For this reason, considerable interest has arisen in the pulp and paper industry concerning the potential replacement of traditional bleaching reagents with en- [Pg.150]


An oxidative activation of the lignin also can be achieved in a biochemical way by adding enzymes (phenol oxidase laccase) to the spent sulfite liquor, whereby... [Pg.1073]

Horse radish peroxidase, H2O2 or Laccase, pH 4, 2% DMSO or DMF. Cleavage occurs by the formation of a phenyldiimide, which decomposes to the acid, nitrogen, and benzene. The laccase method is compatible with the readily oxidized tryptophan and methionine because it does not use peroxide. ... [Pg.450]

Laccase, 6,699 copper, 6,654 cytochrome oxidases concerted electron transfer, 6,683 fungal... [Pg.154]

C13-0112. Fungal laccase is an enzyme found in fungi that live on rotting wood. The enzyme is blue and contains 0.40% by mass copper. The molar mass of the enzyme is approximately 64,000 g/mol. How many copper atoms are there in one molecule of fungal laccase ... [Pg.969]

Kim, J.E. et ah. Putative polyketide synthase and laccase for biosynthesis of auro-fusarin in Gibberella zea, Appl. Environ. Microbiol., 71, 1701, 2005. [Pg.119]

Laccase (PCL) as well as peroxidases (HRP and SBP) induced a new type of oxidative polymerization of the 4-hydroxybenzoic acid derivatives, 3,5-dimethoxy-4-hydroxybenzoic acid (syringic acid) and 3,5-dimethyl-4-hydroxybenzoic acid. The polymerization involved elimination of carbon dioxide and hydrogen from the monomer to give PPO derivatives with molecular weight up to 1.8 x lO (Scheme 22). - ... [Pg.233]

Superoxide anion scavenging activity of the enzymatically synthesized poly(catechin) was evaluated. Poly(catechin), synthesized by HRP catalyst, greatly scavenged superoxide anion in a concentration-dependent manner, and almost completely scavenged at 200 p.M of a catechin unit concentration. The laccase-catalyzed synthesized poly(catechin) also showed excellent antioxidant property. Catechin showed pro-oxidant property in concentrations lower than 300 jlM. These results demonstrated that the enzymatically synthesized poly(catechin) possessed much higher potential for superoxide anion scavenging, compared with intact catechin. [Pg.241]

The conjugation of catechin on poly(allylamine) using ML as catalyst was examined under air. During the conjugation, the reaction mixture turned brown and a new peak at 430 nm was observed in the UV-vis spectrum. At pH 7, the reaction rate was the highest. The conjugation hardly occurred in the absence of laccase, indicating that the reaction proceeded via enzyme catalysis. [Pg.243]

Catechin-immobilizing polymer particles were prepared by laccase-catalyzed oxidation of catechin in the presence of amine-containing porous polymer particles. The resulting particles showed good scavenging activity toward stable free l,l-diphenyl-2-picryl-hydrazyl radical and 2,2 -azinobis(3-ethylbenzothiazoline-6-sulfonate) radical cation. These particles may be applied for packed column systems to remove radical species such as reactive oxygen closely related to various diseases. [Pg.244]

Perez J, TW Jeffries (1990) Mineralization of C-ring-labelled synthetic lignin correlates with the production of lignin peroxidase, not of manganese peroxidase or laccase. Appl Environ Microbiol 56 1806-1812. [Pg.86]

FIGURE 4.8 Reaction between 2,4,5-trichlorophenol and syringic acid catalyzed by laccase. [Pg.207]

Zille A, B Gdrnacka, A Rehorek, A Cavaco-Paulo (2005) Degradation of azo dyes by Trametes villosa laccase over long periods of oxidative conditions. Appl Environ Microbiol 71 6711-6718. [Pg.522]

Laccase active site with proposed mode of substrate / Intermediate binding... [Pg.594]

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.)...
Figure 17.5 The protein environment around the Cu centers (gold spheres) of laccase from Melanocarpus albomyces (PDB file IGWO) showing a substrate O2 molecule bound in the trinuciear Cu site [Hakulinen et al., 2002], The protein is depicted in stick representation with atoms in their conventional coloring. (Courtesy of Armand W. J. W. Tepper.) (See color insert.)... Figure 17.5 The protein environment around the Cu centers (gold spheres) of laccase from Melanocarpus albomyces (PDB file IGWO) showing a substrate O2 molecule bound in the trinuciear Cu site [Hakulinen et al., 2002], The protein is depicted in stick representation with atoms in their conventional coloring. (Courtesy of Armand W. J. W. Tepper.) (See color insert.)...

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Arene Oxidation with Laccases

Bacterial laccases

Biocatalyst laccases

Biotransformations oxidation with laccases

Blood-tolerant laccase

Blue copper oxidases Laccase

Blue copper proteins laccases

Ceriporiopsis subvermispora, laccase

Cerrena unicolor laccase

Copper proteins laccase

CotA laccase

Cytochrome laccase electrode

Direct and catalytic voltammetry of P. versicolor laccase

Directed Evolution of Laccases

Directed Evolution of Medium-Redox Potential Laccases

Enzymatic oxidation, laccase activity

Enzyme laccase

Enzymes Laccase modification

Enzymes laccases

Fungal Laccases, Ascorbate Oxidases, and Related Proteins

High-redox potential laccases

Hydroquinone, laccase-catalyzed

Hydroquinone, laccase-catalyzed reaction

Kinetic Properties of Laccase and Ascorbate Oxidase

Kraft pulping laccase-mediator pretreatment

Laccase

Laccase (LAC

Laccase Rhus vernicifera

Laccase Rhus,

Laccase absorption spectra

Laccase activity assay

Laccase activity unit

Laccase amino-acid sequences

Laccase anaerobic reduction

Laccase analysis

Laccase azide binding

Laccase bacterial

Laccase binding

Laccase biological activity

Laccase biological function

Laccase copper

Laccase copper content

Laccase copper sites

Laccase cytochrome oxidases

Laccase denaturation

Laccase distribution

Laccase electrochemistry

Laccase electrodes

Laccase evolution

Laccase function

Laccase functional molecules from

Laccase fungal

Laccase hemocyanin

Laccase inhibition

Laccase kinetic properties

Laccase kinetic studies

Laccase modification

Laccase multi-copper enzymes

Laccase nature

Laccase occurrence

Laccase peroxy intermediate

Laccase polyporus

Laccase production

Laccase properties

Laccase redox potentials

Laccase reduction reactions

Laccase reoxidation

Laccase sequence alignments with ascorbate

Laccase source

Laccase spectra

Laccase spectroscopy

Laccase trinuclear copper active site

Laccase type 2-depleted

Laccase voltammetry

Laccase, ceruloplasmin electron transfer

Laccase, role

Laccase, testing

Laccase-Initiated Polymerization

Laccase-catalyzed biotransformation

Laccases action mechanism

Laccases active site

Laccases applications

Laccases biomass

Laccases biopolymers

Laccases derivatives

Laccases dimeric

Laccases directed evolution

Laccases ethanol

Laccases food industry

Laccases from Polyporus versicolor

Laccases from Rhus vernicifera

Laccases from Trametes versicolor

Laccases from tree

Laccases glycoside oxidation

Laccases imaging

Laccases immobilization

Laccases lignin degradation

Laccases of Coriolus versicolor

Laccases pathways

Laccases redox

Laccases redox mediators

Laccases sources

Laccases structure

Laccases substrates

Laccases textile industry

Laccases, role

Laccase—mediator system

Ligninolytic high-redox potential laccases

Mediators laccase oxidation

Multicopper laccases

Multicopper oxidases laccases

Organic synthesis laccases

Oxidases, laccase

Oxygen intermediate, laccase

Phenolics laccase-catalyzed polymerization

Physical Properties of Laccases

Polymers laccases

Polyporus anceps, laccase

Polyporus versicolor Laccase

Polyporus versicolor, laccases

Rhus vemicifera laccases

Rhus vernicifera, laccases

Small laccase from Streptomyces

Small laccase from Streptomyces coelicolor

The Mechanism of Laccases

Trametes hirsuta laccase

Trametes versicolor laccase

Trametes villosa, laccase

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