Production of lignin peroxidase and laccase by Phlebia radiata

Kantelinen, Anne; Hatakka, Annele; Viikari, Liisa

doi:10.1007/bf00258401

Cited by 81 publications

(48 citation statements)

References 20 publications

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“…Production of laccase activity by P. radiata in bioreactor cultivations similar to that used for the RNA isolations has been described (Kantelinen et al, 1989). Typically, the laccase activity starts to appear after day 1, reaching its peak value on day 3, after which it starts to decrease.…”

Section: Methodsmentioning

confidence: 99%

Isolation and structural analysis of the laccase gene from the ligninegrading fungus Phlebia radiata

Saloheimo

Niku‐Paavola

Knowles

1991

Journal of General Microbiology

127

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We have isolated and characterized a gene coding for the laccase of the lignin-degrading fungus Phlebia radiaftr, The gene has nine introns and recognizable fungal promoter elements. Sequences homologous to the consensus eukaryotic heat-shock regulatory element can be found in the promoter. RNA hybridization results indicate that this gene is regulated at the transcriptional level. The derived laccase amino acid sequence shows homology to plant ascorbate oxidases, suggesting that the basic structure of the laccase is similar to the three-fold repeated P-barrel of the ascorbate oxidases. Potential copper ligands and a residue carrying the prosthetic group pyrroloquinoline quinone (PQQ) in the laccase protein can be identified by homology. The intron/exon structure of the laccase gene suggests that this protein could have evolved by exon shuffiing.

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Section: Methodsmentioning

confidence: 99%

Isolation and structural analysis of the laccase gene from the ligninegrading fungus Phlebia radiata

Saloheimo

Niku‐Paavola

Knowles

1991

Journal of General Microbiology

127

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“…The fungus was cultivated in 2-1 bioreactors at 28 "C immobilised onto a polypropylene carrier [42, 461 in lownitrogen asparaginefammonium nitrate/dimethylsuccinate medium at pH 4.5 [401 containing 56 mM glucose and 0.05 % (massfvol.) Tween 80 [42,461. Veratric (3,4-dimethoxybenzoic) acid (1.0 mM) was added to enhance production of ligninolytic enzymes [43].…”

Section: Production and Purification Of L3mentioning

confidence: 99%

“…P. rudiutu 79 is a selective and efficient lignindegrader [40] secreting ligninolytic enzymes under conditions similar to those of P. chrysosporium [41,42). However, the ligninolytic system of P. rudiutu differs from that of P. chrysosporium since, in addition to Lip and MnP, P. rudiutu also produces laccase .…”

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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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“…3.2) is a common property amongst basidiomycete fungi. In organisms such as Sporotrichum pulverulentum and Phlebia radiata a function related to lignin degradation has been proposed (Ander & Eriksson, 1976;Kantelinen et al, 1989). A similar function may apply to the constitutively produced laccase of Agaricus bisporus (Wood, 1985).…”

Section: Introductionmentioning

confidence: 99%

Purification of laccase I from Armillaria mellea

Rehman¹,

Thurston

1992

Journal of General Microbiology

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Laccase activity accumulated during rhizomorph development in malt extract cultures of Armillaria meffeu. The activity was readily separated into two bands by PAGE under non-denaturing conditions. The less rapidly migrating activity (on PAGE) was purified by ammonium sulphate precipitation, anion-exchange chromatography and gel filtration. The purified enzyme (laccase I) showed a main polypeptide of M,. 59000. Activity of the purified enzyme was greatest with 2,6-dimethoxyphenol (DMOP) as substrate. Syringaldazine, p-phenylenediamine and other typical laccase substrates were readily oxidized. No oxidation of tyrosine was detected. The K, for DMOP was 0.178 mM and for p-phenylenediamine was 1.69 mM. The pH optimum for pphenylenediamine oxidation was 3.5. Electrophoretically purified main polypeptide of laccase I was used to raise a specific antibody. Immunoblot analysis showed that whilst the antibody bound strongly to laccase I, no binding to laccase I1 was detectable.Antibody raised against pure laccase from Agaricus bisporus reacted with laccase I from Armillaria meffeu but not with laccase 11. The isolectric pH was 4.1 for laccase I and 3.3 for laccase 11.

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Production of lignin peroxidase and laccase by Phlebia radiata

Cited by 81 publications

References 20 publications

Isolation and structural analysis of the laccase gene from the ligninegrading fungus Phlebia radiata

Isolation and structural analysis of the laccase gene from the ligninegrading fungus Phlebia radiata

Lignin peroxidase L3 from Phlebia rediata

Purification of laccase I from Armillaria mellea

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