On the Mechanism of Oxidation of Non-Phenolic Lignin Model Compounds by the Laccase-ABTS Couple

Muheim, Andreas; Fiechter, Armin; Harvey, Patricia J.

doi:10.1515/hfsg.1992.46.2.121

Cited by 77 publications

(50 citation statements)

References 11 publications

(14 reference statements)

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“…21,22 However, their inertness in the presence of radical mediators was unexpected. In fact, it has been reported that the radical mediator ABTS is able to bring about the oxidation of non-phenolic systems characterized by a redox potential higher than laccase such as veratryl alcohol or non-phenolic b-O-4 model compounds.…”

Section: Discussionmentioning

confidence: 99%

The early oxidative biodegradation steps of residual kraft lignin models with laccase

Crestini

Argyropoulos

1998

Bioorganic & Medicinal Chemistry

129

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Section: Discussionmentioning

confidence: 99%

The early oxidative biodegradation steps of residual kraft lignin models with laccase

Crestini

Argyropoulos

1998

Bioorganic & Medicinal Chemistry

129

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“…This suggests that laccases may be capable of catalyzing all of the necessary oxidative processes required for complete degradation of lignin in vivo if white-rot fungi also produce some compound as a physiological redox-mediator. Kawai et al (42) reported that syringaldehyde might function as such a physiological redox-mediator for laccase-catalyzed lignin degradation; however, these results have proven difficult to reproduce (43). Thus, (at this point) the existence, not to mention the identity, of physiological redox-mediators produced by white-rot fungi in vivo remained to be demonstrated.…”

Section: Mn-inhibited Peroxidase 'Information Not Givenmentioning

confidence: 97%

Laccase-Producing White-Rot Fungus Lacking Lignin Peroxidase and Manganese Peroxidase

Eggert

Temp

Eriksson

1996

ACS Symposium Series

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This paper presents an overview of phenoloxidases involved in lignin degradation with a particular focus on laccase. To investigate the role of laccase in lignin degradation, Pycnoporus cinnabarinus was identified as an excellent organisms for further study. It produces only one isoelectric form of laccase and yet degrades lignin fast and extensively. We report here on the purification and characterization of the P. cinnabarinus laccase. Laccases are generally considered to have a too low redox potential to attack non-phenolic lignin substrates. This is also true for the laccase from P. cinnabarinus. However, to make up for this deficiency, P. cinnabarinus was found to produce a redox mediator, 3-hydroxy anthranilic acid (3-HAA). Laccase plus the redox mediator, was demonstrated to degrade a non-phenolic lignin model dimer.Lignins constitute the second most abundant group of biopolymers in the biosphere; thus, their biodégradation occupies an important position in the global carbon cycle. Studies of lignin biodégradation are also of great importance for possible biotechnological applications since lignin polymers are a major obstacle to the efficient utilization of lignocellulosic materials in a wide range of industrial processes (I). The turnover of lignin biomass occurs primarily through the action of white-rot fungi, consequently, this ecological group has received a considerable amount of research attention, as have the enzymatic mechanisms employed by these fungi for the breakdown of lignin.Most of our understanding of the enzymology of lignin biodégradation stems from studies of a single species of white-rot fungus, Phanerochaete chrysosporium. In P. chrysosporium, lignin degradation occurs only after secondary metabolism has been triggered by starvation for nitrogen, sulfur or phosphorus (2). Prodigious production of extracellular phenoloxidases is a characteristic of this ligninolytic metabolism, and was noted even in very early studies of the differences between 0097-6156/96/0655-0130$15.25/0

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“…Laccases are able to catalyse phenoxy radical formation from phenolic substances, but have also been shown to effect the oxidation of non-phenolic compounds by a laccase-substrate couple which does not appear to proceed via radical cation intermediates (Bourbonnais and Paice, 1990;Muheim et al, 1992). In our study, we monitored the development and electrophoretic variations of iaccase during the decolourisation of RBBR in a bioreactor.…”

Section: Introductionmentioning

confidence: 99%

Laccase variation during dye decolourisation in a 200 L packed-bed bioreactor

Schliephake

Lonergan

1996

Biotechnol Lett

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The white-rot fungus, Pycnoporus cinnabarinus, was grown in a 200 L packed-bed bioreactor. The dye, Remazol Brilliant Blue R, was added to the reactor and was rapidly decolourised. The phenoloxidase, laccase, catalysed this process. Laccases isolated from different days in the bioreactor cycle indicated variations in charge to size characteristics. Purified laccase from different days was isoelectrically focused and showed variations in intensities and numbers of bands whilst catalytic activity was retained.

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On the Mechanism of Oxidation of Non-Phenolic Lignin Model Compounds by the Laccase-ABTS Couple

Cited by 77 publications

References 11 publications

The early oxidative biodegradation steps of residual kraft lignin models with laccase

The early oxidative biodegradation steps of residual kraft lignin models with laccase

Laccase-Producing White-Rot Fungus Lacking Lignin Peroxidase and Manganese Peroxidase

Laccase variation during dye decolourisation in a 200 L packed-bed bioreactor

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