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Pycnoporus cinnabarinus

Figure 17.7 Electrocatalysis of O2 reduction by Pycnoporus cinnabarinus laccase on a 2-aminoanthracene-modified pyrolytic graphite edge (PGE) electrode and an unmodified PGE electrode at 25 °C in sodium citrate buffer (200 mM, pH 4). Red curves were recorded immediately after spotting laccase solution onto the electrode, while black curves were recorded after exchanging the electrochemical cell solution for enzyme-fiiee buffer solution. Insets show the long-term percentage change in limiting current (at 0.44 V vs. SHE) for electrocatalytic O2 reduction by laccase on an unmodified PGE electrode ( ) or a 2-aminoanthracene modified electrode ( ) after storage at 4 °C, and a cartoon representation of the probable route for electron transfer through the anthracene (shown in blue) to the blue Cu center of laccase. Reproduced by permission of The Royal Society of Chemistry fi om Blanford et al., 2007. (See color insert.)... Figure 17.7 Electrocatalysis of O2 reduction by Pycnoporus cinnabarinus laccase on a 2-aminoanthracene-modified pyrolytic graphite edge (PGE) electrode and an unmodified PGE electrode at 25 °C in sodium citrate buffer (200 mM, pH 4). Red curves were recorded immediately after spotting laccase solution onto the electrode, while black curves were recorded after exchanging the electrochemical cell solution for enzyme-fiiee buffer solution. Insets show the long-term percentage change in limiting current (at 0.44 V vs. SHE) for electrocatalytic O2 reduction by laccase on an unmodified PGE electrode ( ) or a 2-aminoanthracene modified electrode ( ) after storage at 4 °C, and a cartoon representation of the probable route for electron transfer through the anthracene (shown in blue) to the blue Cu center of laccase. Reproduced by permission of The Royal Society of Chemistry fi om Blanford et al., 2007. (See color insert.)...
Schliephake K, Mainwaring DE, Lonergan GT, Jones KI, Baker WL (2000) Transformation and degradation of the disazo dye Chicago sky blue by a purified laccase from Pycnoporus cinnabarinus. Enzyme Microb Biotechnol 27 100-107... [Pg.168]

In Phanerochaete flavido-alba, an induction of ligninolytic activities that was ascribed to phenolic compounds was evidenced [69]. Phenols have also been shown to have an important role as redox mediators for dye degradation with laccases from Pycnoporus cinnabarinus and Trametes villosa, and they resulted to be necessary to degrade a strongly recalcitrant azo dye, the Reactive Black 5 [70]. [Pg.204]

At least 87 basidiomycete heme peroxidases have been described to date, whose evolutionary relationships are shown in Fig. 3.3. It also includes putative peroxidases from the genomes of Phanerochaete chrysosporium, Pleurotus ostreatus. and Pycnoporus cinnabarinus, and two reference ascomycete peroxidases. [Pg.44]

Bonnin, E. et al., Aspergillus niger 1-1472 and Pycnoporus cinnabarinus MUCEL 39533, selected for the biotransformation of ferulic acid to vanillin, are also able to produce cell wall polysaccharide-degrading enzymes and feruloyl esterases, Enzyme Microb. Technol, 28, 70, 2001. [Pg.251]

C Eggert, U Temp, KEL Eriksson. Laccase is essential for lignin degradation by the white-rot fungus Pycnoporus cinnabarinus. FEBS Lew 407(1 ) 89-92, 1997. [Pg.548]

K Li, PS Horanyi, R Collins, RS Phihips, K-EL Eriksson. Investigation of the role of 3-hydroxyanthranilic acid in the degradation of lignin by white-rot fungus Pycnoporus cinnabarinus. Enzyme Microb. Technol. 28(4—5) 301-307, 2001. [Pg.552]

Also in the polyporaceous fungus, Pycnoporus cinnabarinus, the conversion of HA to CA has been shown, even if there is no Mn2+ requirement for the process [194]. The same was seen also in extracts of spinach leaves [195]. Nuclear fractions, coming from other rat organs, were found able to catalyse the conversion of HA to CA [195], Nucleotide bases, and in particular guanine, behave as competitive inhibitors for the conversion, and this fact, together with the strict structural analogies between... [Pg.1010]

Sigoillot, C., Lomascolo, A., Record, E., Robert, J. L., Asther, M., Sigoillot, J. C. (2002). Lignoeellulolytic and hemicellulolytic system of Pycnoporus cinnabarinus isolation and characterization of a cellobiose dehydrogenase and a new xylanase. Enzyme and Microbial Technology, 31, 876-883. [Pg.165]

Madzak, C., Otterbein, L., Chamkha, M., Moukha, S., et al.. Heterologous production of a laccase from the basidiomycete Pycnoporus cinnabarinus in the dimorphic yeast Yarrowia lipolytica, FEMS Yeast Res. 2005, 5, 635-646. [Pg.180]

Ferulic acid is the major cinnamic acid found in a variety of plant cell walls. Com fiber contains about 3% femlic acid. Wheat bran is another source of ferulic acid (0.5-1%). Faulds et al. 226) developed a laboratory scale procedure to produce free femlic acid (5.7 g) from wheat bran (1 kg) by using a Trichoderma xylanase preparation and A, niger femlic acid esterase. Using filamentous fungi, a two-stage process for vanillin formation was developed in which a strain of A. niger was first used to convert femlic acid to vanillic acid, which was then reduced to vanillin by a laccase-deficient strain of Pycnoporus cinnabarinus 227). [Pg.24]

Degradation of Wood and Pulp by Three Fungi, Pycnoporus cinnabarinus, Trichophyton rubrum LKY-7 and Trichophyton rubrum LSK-27... [Pg.139]

Substituted phenoxazin-3-one pigments impart the very stable bright orange-red colour to the conspicuous bracket shaped fruit bodies of the wood-rotting fungi Pycnoporus cinnabarinus, P, sanguineus and P. coccineus (Table 45). [Pg.208]

Also, a two-step process was patented in 1996 [49], employing two different filamentous fungi Aspergillus niger and Pycnoporus cinnabarinus. In the first step, A. niger transformed ferulic acid to vanillic acid, and in the second step the latter was reduced to vanillin by P. cinnabarinus [50]. The yields have been improved to over 0.5 gl adding cellobiose to the culture medium [51]. This behavior has been ascribed either to the fact that cellobiose is a more easily metabolized carbon source, required for the reduction to occur, or to its action as an inducer of cellobiose-quinone oxidoreductase, which inhibits vanillic acid decarboxylation. [Pg.280]

Lesage-Meessen, L., Haon, M., Delattre, M., Ihibault, J.F., Colonna Ceccaldi, B., and Ashter, M. (1997) An attempt to channel the transformation of vanillic acid into vanillin by controlling methoxyhydroquinone formation in Pycnoporus cinnabarinus with cel-lobiose. Appl. Microbiol. Biotechnol.,... [Pg.300]

Lomascolo, A., Lesage-Meessen, L., Labat, M., Navarro, D., Delattre, M., and Asther, M. (1999) Enhanced benzaldehyde formation by a monokaryotic strain of Pycnoporus cinnabarinus using a selective solid adsorbent in the culture medium. Carr J. Microbiol, 45,... [Pg.302]


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Vanillin Pycnoporus cinnabarinus

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