Pleurotus eryngii

Guillen F, AT Martinez, MJ Martinez (1992) Substrate specificity and properties of the aryl-alcohol oxidase from the ligninolytic fungus Pleurotus eryngii. Eur J Biochem 209 603-611. [Pg.138]

Aryl alcohol oxidase from the ligninolytic fungus Pleurotus eryngii had a strong preference for benzylic and allylic alcohols, showing activity on phenyl-substituted benzyl, cinnamyl, naphthyl and 2,4-hexadien-l-ol [103,104]. Another aryl alcohol oxidase, vanillyl alcohol oxidase (VAO) from the ascomycete Penicillium simplicissimum catalyzed the oxidation of vanillyl alcohol and the demethylation of 4-(methoxymethyl)phenol to vanillin and 4-hydro-xybenzaldehyde. In addition, VAO also catalyzed deamination of vanillyl amine to vanillin, and hydroxylation and dehydrogenation of 4-alkylphenols. For the oxidation of 4-alkylphenol, the ratio between the alcohol and alkene product depended on the length and bulkiness of the alkyl side-chain [105,106]. 4-Ethylphenol and 4-propylphenol, were mainly converted to (R)-l-(4 -hydroxyphenyl) alcohols, whereas medium-chain 4-alkylphenols such as 4-butylphenol were converted to l-(4 -hydroxyphenyl)alkenes. [Pg.158]

Varela, E., Guillen, F., Martinez, A.T. and Martinez, M.J. (2001) Expression of Pleurotus eryngii aryl-alcohol oxidase in Aspergillus nidulans purification and characterization of the recombinant enzyme. Biochimica et Biophysica Acta, Protein Structure and Molecular, Enzymology, 1546 (1), 107-113. [Pg.166]

VP (E.C. 1.11.1.46) was first described in liquid cultures of Pleurotus eryngii growing on peptone as nitrogen source [82, 83] and Bjerkandera sp. [84], VP is a heme containing structural hybrid between MnP and LiP, as it is able to oxidize Mn2+, veratryl alcohol, simple amines, phenolic, nonphenolic and high molecular... [Pg.143]

White rot fungi, namely Phanerochaete chrysosporium, Pleurotus sajorcaju, Pleurotus florida, and Pleurotus eryngii, biodegraded heptachlor (50 pM) at degradation yields of 92.13 to 97.30, 59.53 to 84.76, 66.25 to 80.00, and 85.85 to 95.15%, respectively. The experiments were... [Pg.612]

Ruiz-Duenas FJ, Morales M, Perez-Boada M et al (2007) Manganese oxidation site in Pleurotus eryngii versatile peroxidase A site-directed mutagenesis, kinetic and crystallographic study. Biochemistry 46 66-77... [Pg.55]

Fleinfling A, Martinez MJ, Martinez AT et al (1998) Transformation of industrial dyes by manganese peroxidase from Bjerkandera adusta and Pleurotus eryngii in a manganese-independent reaction. Appl Environ Microbiol 64 2788-2793... [Pg.57]

Pogni R, Baratto MC, Teutloff C et al (2006) A tryptophan neutral radical in the oxidized state of versatile peroxidase from Pleurotus eryngii a combined multi-frequency EPR and DFT study. J Biol Chem 281 9517-9526... [Pg.58]

Ruiz-Duenas FJ, Morales M, Mate MJ et al (2008) Site-directed mutagenesis of the catalytic tryptophan environment in Pleurotus eryngii versatile peroxidase. Biochemistry 47 1685-1695... [Pg.58]

Fleinlling A, Ruiz-Duenas FJ, Martinez MJ et al (1998) A study on reducing substrates of manganese-oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta. FEBS Lett 428 141-146... [Pg.59]

In some enzymes, the protein radical appears to participate in substrate oxidation. Evidence exists for the involvement of a surface tryptophan in the oxidation of veratryl alcohol by the ligninase from Phanerochaete chrysosporium [33]. Similarly, tryptophan radicals on the surface of the versatile peroxidases from Pleurotus eryngii and Bjerkandera adjusta [34—36], and a tyrosine in the LiP from Trametes cervina [33], are thought to be involved in substrate oxidation. [Pg.85]

MnPL2 Pleurotus eryngii A. nidulans Active protein, heme addition [36]... [Pg.321]

CPO Chloroperoxidase LiP Lignin peroxidase MnP Manganese peroxidase MnPL2 Pleurotus eryngii manganese peroxidase CiP Coprinus cinereus peroxidase ARP Arthromyces ramosus peroxidase VPO Versatile peroxidase DyP dye-decolorizing peroxidase... [Pg.321]

Ruiz-Duenas FJ, Martinez MJ, Martinez AT (1999) Heterologous expression of Pleurotus eryngii peroxidase confirms its ability to oxidize Mn(2+) and different aromatic substrates. Appl Environ Microbiol 65 4705-4707... [Pg.331]

Eibes GM, Lu-Chau TA, Ruiz-Duenas FJ et al (2009) Effect of culture temperature on the heterologous expression of Pleurotus eryngii versatile peroxidase in Aspergillus hosts. Bioprocess Biosyst Eng 32 129-134... [Pg.331]

Veratryl alcohol 240 3.5 68.6 Estimated fox Pleurotus eryngii ATCC 90787 PS1 isoenzyme. Mn2+ [65]... [Pg.342]

Martinez MJ, Ruiz-Duenas FJ, Guillen F et al (1996) Purification and catalytic properties of two manganese peroxidase isoenzymes from Pleurotus eryngii. Eur J Biochem 237 424—432... [Pg.350]

An aryl-alcohol oxidase produced optimally under carbon limitation from Bjerkandera adusta oxidized a number of benzyl alcohols including 4-methoxybenzyl alcohol, 3,4-dimethoxybenzyl alcohol (veratryl alcohol), and 4-hydroxy-3-methoxybenzyl alcohol, with the production of H202 from 02 monosaccharides were not oxidized (Muheim et al. 1990). An aryl-alcohol oxidase from Pleurotus eryngii is a flavoprotein with range of substrates comparable to that from B. adusta (Guillen et al. 1992). [Pg.310]

Spawn of these species available Pleurotus ostreatus Pleurotus sajor-caju Pleurotus cornucopiae Pleurotus eryngii Lentinus edodes and Stropharia rugoso-annulata. [Pg.384]

Synytsya, A., Mfckova, K., Synytsya, A., Jablonsky, I., Spevacek, J., Erban, V., Kovankova, E., and J. Copikova. 2009. Glucans from fruit bodies of cultivated mushrooms Pleurotus ostreatus and Pleurotus eryngii Structure and potential prebiotic activity. Carbohydrate Polymers 76 548-556. [Pg.10]

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