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Registros recuperados: 7
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Cloning and characterization of a tyrosinase gene from the white-rot fungus Pycnoporus sanguineus, and overproduction of the recombinant protein in Aspergillus niger Inra
Halaouli, S.; Record, E.; Casalot, L.; Hamdi, M.; Sigoillot, J.C.; Lomascolo, A.; Asther, M..
A new tyrosinase-encoding gene (2,204 bp) andthe corresponding cDNA (1,857 nucleotides) from thewhite-rot fungus Pycnoporus sanguineus BRFM49 werecloned. This gene consisted of seven exons and six intronsand encoded a predicted protein of 68 kDa, exceeding themature tyrosinase by 23 kDa. P. sanguineus tyrosinasecDNA was over-expressed in Aspergillus niger, a particularlysuitable fungus for heterologous expression of proteinsof biotechnological interest, under the control ofthe glyceraldehyde-3-phosphate-dehydrogenase promoteras strong and constitutive promoter. The glucoamylasepreprosequence of A. niger was used to target the secretion.This construction enabled the production of recombinanttyrosinase in the extracellular medium of A. niger. Theidentity of...
Tipo: Journal Article Palavras-chave: FUNGAL TYROSINASE.
Ano: 2006 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20078d7fe834&uri=/notices/prodinra1/2010/09/
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Comparison of the characteristics of fungal and plant tyrosinases Inra
Selinheimo, E.; NiEidhin, D.; Steffensen, C.; Nielsen, J.; Lomascolo, A.; Halaouli, S.; Record, E.; O’Beirne, D.; Buchert, J.; Kruus, K..
Enzymatic crosslinking provides valuable means for modifying functionality and structural properties of different polymers. Tyrosinases catalyze the hydroxylation of various monophenols to the corresponding o-diphenols, and the subsequent oxidation of o-diphenols to the corresponding quinones, which are highly reactive and can further undergo non-enzymatic reactions to produce mixed melanins and heterogeneous polymers. Tyrosinases are also capable of oxidizing protein- and peptide-bound tyrosyl residues, resulting in the formation of inter- and intra-molecular crosslinks. Tyrosinases from apple (AT), potato (PT), the white rot fungus Pycnoporus sanguineus (PsT), the filamentous fungus Trichoderma reesei (TrT) and the edible mushroom Agaricus bisporus (AbT)...
Tipo: Journal Article Palavras-chave: ENZYME; SPECTROSCOPIE; ACTIVITE ENZYMATIQUE; INHIBITION ENZYMATIQUE PYCNOPORUS SANGUINEUS; TRICHODERMA REESI.
Ano: 2007 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2008c0091e56&uri=/notices/prodinra1/2008/06/
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Evidence of a new biotransformation pathway of p-coumaric acid into p-hydroxybenzaldehyde in Pycnoporus cinnabarinus Inra
Estrada Alvarado, I.; Lomascolo, A.; Navarro, D.; Delattre, M.; Asther, M.; Lesage-Meessen, L..
Pycnoporus cinnabarinus MUCL39533 was shown to be able to convert p-coumaric acid into p-hydroxybenzaldehyde, a component of high organoleptic note present in natural vanilla aroma. Use of phospholipid-enriched medium led to high-density cultures of P. cinnabarinus, since dry mycelial biomass was increased three-fold as compared to glucose medium. In the presence of phospholipids, 155 mg l–1 p-hydroxybenzaldehyde was produced as the major compound on culture day 13 with a molar yield of 26%. The degradation pathways of p-coumaric acid were investigated. Based on the different metabolites identified, an oxidative side-chain degradation pathway of p-coumaric acid conversion to p-hydroxybenzoic acid was suggested. This acid was further reduced...
Tipo: Journal Article Palavras-chave: PYCNOPORUS CINNABARINUS; AROME NATUREL; BENZALDEHYDE; VANILLINE.
Ano: 2001 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0300030628096328&uri=/notices/prodinra1/2010/09/
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One fungus, which genes? Development and assessment of universal primers for potential secondary fungal DNA barcodes Naturalis
Stielow, J.B.; Lévesque, C.A.; Seifert, K.A.; Meyer, W.; Irinyi, L.; Smits, D.; Renfurm, R.; Verkley, G.J.M.; Groenewald, M.; Chaduli, D.; Lomascolo, A.; Welti, S.; Lesage-Meessen, L.; Favel, A.; Al-Hatmi, A.M.S.; Damm, U.; Yilmaz, N.; Houbraken, J.; Lombard, L.; Quaedvlieg, W.; Binder, M.; Vaas, L.A.I.; Vu, D.; Yurkov, A.; Begerow, D.; Roehl, O.; Guerreiro, M.; Fonseca, A.; Samerpitak, K.; Diepeningen, A.D. van; Dolatabadi, S.; Moreno, L.F.; Casaregola, S.; Mallet, S.; Jacques, N.; Roscini, L.; Egidi, E.; Bizet, C.; Garcia-Hermoso, D.; Martin, M.P.; Deng, S.; Groenewald, J.Z.; Boekhout, T.; Beer, Z.W. de; Barnes, I.; Duong, T.A.; Wingfield, M.J.; Hoog, G.S. de; Crous, P.W.; Lewis, C.T.; Hambleton, S.; Moussa, T.A.A.; Al-Zahrani, H.S.; Almaghrabi, O.A.; Louis-Seize, G.; Assabgui, R.; McCormick, W.; Omer, G.; Dukik, K.; Cardinali, G.; Eberhardt, U.; Vries, M. de; Robert, V..
The aim of this study was to assess potential candidate gene regions and corresponding universal primer pairs as secondary DNA barcodes for the fungal kingdom, additional to ITS rDNA as primary barcode. Amplification efficiencies of 14 (partially) universal primer pairs targeting eight genetic markers were tested across > 1 500 species (1 931 strains or specimens) and the outcomes of almost twenty thousand (19 577) polymerase chain reactions were evaluated. We tested several well-known primer pairs that amplify: i) sections of the nuclear ribosomal RNA gene large subunit (D1–D2 domains of 26/28S); ii) the complete internal transcribed spacer region (ITS1/2); iii) partial β-tubulin II (TUB2); iv) γ-actin (ACT); v) translation elongation factor 1-α (TEF1α);...
Tipo: Article / Letter to the editor Palavras-chave: DNA barcoding; ITS supplement; Molecular taxonomy; Phylogeny; Species identification; Universal primers.
Ano: 2015 URL: http://www.repository.naturalis.nl/record/588731
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Oxidative degradation of model lipids representative for main paper pulp lipophilic extractives by the laccase-mediator system Inra
Molina, S.; Rencoret, J.; del Rio, J.C.; Lomascolo, A.; Record, E.; Martinez, A.T.; Gutierrez, A..
Different model lipids—alkanes, fatty alcohols,fatty acids, resin acids, free sterols, sterol esters, andtriglycerides—were treated with Pycnoporus cinnabarinuslaccase in the presence of 1-hydroxybenzotriazole asmediator, and the products were analyzed by gas chromatography.The laccase alone decreased the concentration ofsome unsaturated lipids. However, the most extensive lipidmodification was obtained with the laccase–mediatorsystem. Unsaturated lipids were largely oxidized and thedominant products detected were epoxy and hydroxy fattyacids from fatty acids and free and esterified 7-ketosterolsand steroid ketones from sterols and sterol esters. Theformer compounds suggested unsaturated lipid attack viathe corresponding hydroperoxides. The enzymatic...
Tipo: Journal Article Palavras-chave: ACTIVITE ENZYMATIQUE OXIDATIVE ENZYME; GAS CHROMATOGRAPHY; LACCASE-MEDIATOR SYSTEM; FUNGAL ENZYME; MODEL LIPIDS; REACTION MECHANISMS; PAPER PULP; PITCH DEPOSITS.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2008c803f667&uri=/notices/prodinra1/2010/09/
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Role of ethanol on growth, laccase production and protease activity in Pycnoporus cinnabarinus ss3 Inra
Meza, J.C.; Auria, R.; Lomascolo, A.; Sigoillot, J.C.; Casalot, L..
Laccase production by the strain Pycnoporus cinnabarinus ss3 was studied in a solid-state culture on sugar-cane bagasse using chemical compounds as inducers (ethanol, methanol, veratryl alcohol and ferulic acid). Laccase productions were about 5- to 8.5-fold higher than non-induced cultures.Liquid-culture experiments with 14C-labeled ethanol were conducted. Ninety-eight percent of the initial amount of 14C from ethanol was recovered as 14CO2, 14C-biomass and soluble 14C-compounds (mainly ethanol). The amount of 14C in the biomass was only 6.8% of the total carbon consumed by P. cinnabarinus, in absence of maltose, representing only 2.8% of added ethanol (1.1% and 1.6% in presence of maltose, respectively). Ethanol was poorly used as carbon and energy...
Tipo: Journal Article Palavras-chave: ENZYME PROTEOLYTIQUE; ACTIVITE ENZYMATIQUE PYCNOPORUS CINNABARINUS.
Ano: 2007 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20086cc0fa6a&uri=/notices/prodinra1/2008/06/
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Transgenic rice as a novel production system for Melanocarpus and Pycnoporus laccases Inra
de Wilde, C.; Uzan, E.; Zhou, Z.; Kruus, K.; Andberg, M.; Buchert, J.; Record, E.; Asther, M.; Lomascolo, A..
Laccases have numerous biotechnological applications, among them food processing. The widespread use of laccases has increased the demand for an inexpensive and safe source of recombinant enzyme. We explored the use of a rice-based system for the production of two fungal laccases derived from the ascomycete Melanocarpus albomyces and the basidiomycete Pycnoporus cinnabarinus. High-expression levels of active recombinant laccases were achieved by targeting expression to the endosperm of rice seeds. The laccase cDNAs were fused to a plant-derived signal sequence for targeting to the secretory pathway, and placed under the control of a constitutive seed-specific promoter fused to an intron for enhanced expression. This construct enabled the recovery of on...
Tipo: Journal Article Palavras-chave: PLANTE TRANSGENIQUE; BIOTECHNOLOGIE INDUSTRIELLE; PROPRIETE BIOCHIMIQUE; ASCOMYCETE; BASIDIOMYCETE LACCASE; RECOMBINANT FUNGAL ENZYME; RICE; HETEROLOGOUS PROTEIN; TRANSGENIC PLANT; BIOCHEMICAL PROPERTIES.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2008c973f6c6&uri=/notices/prodinra1/2008/10/
Registros recuperados: 7
Primeira ... 1 ... Última
 

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