Separation and characterization of two extracelluar H2O2‐dependent oxidases from ligninolytic cultures of Phanerochaete chrysosporium

Kuwahara, Masaaki; Glenn, Jeffrey K.; Morgan, Meredith A.; Gold, Michael H.

doi:10.1016/0014-5793(84)80327-0

Cited by 782 publications

(367 citation statements)

References 13 publications

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“…One unit [U] was defined as the amount of enzyme that oxidised 1 µmol of veratryl alcohol in 1 min, and the activities were reported as U/l. Mn (II)-Dependent Peroxidase was assayed spectrophotometrically by the method of KUWAHARA et al [20]. One activity unit [U] was defined as the amount of enzyme that oxidised 1 µmol of dimethoxyphenol per minute, and the activities were expressed in U/l.…”

Section: Methodsmentioning

confidence: 99%

Biodegradation of Grape Cluster Stems and Ligninolytic Enzyme Production by Phanerochaete chrysosporium during Semi‐Solid‐State Cultivation

Couto

Rodríguez

Gallego

et al. 2003

Acta Biotechnologica

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SummaryThe degradation undergone by grape cluster stems (woody component of vine bagasse), an agroindustrial waste, was investigated during the semi-solid-state cultivation of Phanerochaete chrysosporium BKM-F-1767 (ATCC 24725). For this, the content of lignin, cellulose and hemicellulose in grape cluster stems was determined before and after the enzymatic process. It was found that about 20% of KLASON lignin, 48% of hemicellulose and 5% of cellulose were degraded during the process, being the ligninolytic enzymes (manganese-dependent peroxidase and lignin peroxidase) produced by such cultures responsible for the degradation of grape cluster stems. In parallel, semi-solid-state cultures of P. chrysosporium grown on an inert support (cubes of nylon sponge), which is not susceptible to undergoing degradation during the enzymatic process, were used as reference cultures. In addition, the in vivo decolourisation of a model dye, the polymeric dye Poly R-478, by both grape cluster stem and nylon cultures was studied in order to assess their degradative ability. A percentage of biological decolourisation higher than 90% after four days of dye addition was obtained using nylon sponge cultures, whereas grape cluster stem cultures led to a decolourisation of around 70% after eight days of dye incubation. The lower percentage of dye degradation achieved by the cultures grown on grape cluster stems was due to the enzymes produced, which were not only employed in the decolourisation of the dye but also in the degradation of the support, as indicated by the data mentioned above.

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Section: Methodsmentioning

confidence: 99%

Biodegradation of Grape Cluster Stems and Ligninolytic Enzyme Production by Phanerochaete chrysosporium during Semi‐Solid‐State Cultivation

Couto

Rodríguez

Gallego

et al. 2003

Acta Biotechnologica

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“…Thus far, most kinetic investigations have been carried out using the Lip isozyme H8 [33]. In addition to Lip, a second heme-peroxidase is produced during ligninolysis, the manganese-dependent or manganese peroxidase (MnP) [35,361, sonamed because of its dependence on both H,O, and manganese for catalysis.…”

mentioning

confidence: 99%

Lignin peroxidase L3 from Phlebia rediata

Lundell

Wever

Floris

et al. 1993

European Journal of Biochemistry

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The catalytic cycle of lignin peroxidase (Lip, ligninase) isozyme L3 from the white-rot fungus Phlebia radiata was investigated using stopped-flow techniques. Veratryl (3,4-dimethoxybenzyl) alcohol and a lignin model compound, non-phenolic a-0-4 dimer 1 -(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol, were used as electron donors. This is the first report on the detailed kinetic analysis of a Lip-catalysed Ca-CB bond cleavage of the dimer, representing the major depolymerisation reaction in the lignin polymer. The native enzyme showed a typical heme peroxidase absorbance spectrum with a Soret maximum at 407 nm. Following the reaction with H,Oz, the Soret band decreased in absorbance, shifted to 403 nm and then to 421 nm, demonstrating the formation of compound I followed by the formation of compound 11, respectively. Similar results have been reported for the Lip from Phunerochaete chrysosporium upon reaction with H,O,. However, compound I of L3 was more stable in the absence of additional electron donors. Thesecond-order rate constant of compound I formation by H,O, was determined to be 6 X IOI M-' s-' and was the same at pH 3.0 and 6.0. Compound I was rapidly reduced to compound Il and further to native enzyme when either veratryl alcohol or the p-0-4 dimer was supplied as electron donor and in both cases veratraldehyde appeared as the major product. At pH 6.0, the second-order rate constant for compound I1 formation was similar with either veratryl alcohol or the p-0-4 dimer (6.7 X lo3 and 6.5 X 103 M-' s-', respectively). At pH 3.0 formation of compound I1 with either reductant proceeded so rapidly that determination of the respective rate constants was not possible. The results point to identical catalytic cycles of L3 with veratryl alcohol or the p-0-4 dimer involving both compounds I and I1 as intermediates and participation of the same veratryl alcohol radical as the most appropriate reductant for compound 11. Chemical evidence of such a radical, formed after the initial Lip-catalysed one-electron oxidation of p-0-4 dimeric lignin models, is presented in a separate article [Lundell, T., Schoemaker, H., Hatakka, A. & Brunow, G. (1993) Holgorschung, in the press]. The catalytic redox-cycle and the oxidation mechanism presented here reconcile seemingly contradictory results obtained in previous studies on Lip kinetics during the last decade.Lignin peroxidase (Lip, ligninase) is an extracellular lignin-degrading enzyme, first discovered in the white-rot fungus Phanerochaete chrysosporium Burds. [I, 21. The enzyme is a glycoprotein that typically has molecular mass of

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“…Para manganês peroxidase (MnP), o método utilizado foi o do vermelho de fenol como substrato, em que a absorbância para leitura foi 610 nm, e a atividade de MnP expressa como ∆Abs.mL -1 .min -1 (KUMAHARA et al, 1984). A atividade enzimá-tica de lignina peroxidase (LiP) foi determinada pela oxidação do álcool veratrílico (ε 310nm =93000 mmol.L -1 .cm -1 ) (TIEN & KIRK,…”

Section: Determinação Da Atividade Enzimáticaunclassified

Estudo da descoloração do corante FD&C azul no 2 Indigotina pelo tratamento combinado do fungo Trametes versicolor e processo de filtração lenta

Lopes

Sales

Campos

et al. 2014

Eng. Sanit. Ambient.

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Separation and characterization of two extracelluar H₂O₂‐dependent oxidases from ligninolytic cultures of Phanerochaete chrysosporium

Cited by 782 publications

References 13 publications

Biodegradation of Grape Cluster Stems and Ligninolytic Enzyme Production by Phanerochaete chrysosporium during Semi‐Solid‐State Cultivation

Biodegradation of Grape Cluster Stems and Ligninolytic Enzyme Production by Phanerochaete chrysosporium during Semi‐Solid‐State Cultivation

Lignin peroxidase L3 from Phlebia rediata

Estudo da descoloração do corante FD&C azul no 2 Indigotina pelo tratamento combinado do fungo Trametes versicolor e processo de filtração lenta

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