Results 151 to 160 of about 8,954 (206)

Bioreduction of selenite and tellurite by Phanerochaete chrysosporium [PDF]

, 2021
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Effect of inoculated azotobacteria and Phanerochaete chrysosporium on the composting of olive pomace: Microbial community dynamics and phenols evolution. [PDF]

Sci Rep, 2019
Milanović V, Osimani A, Cardinali F, Taccari M, Garofalo C, Clementi F, Ashoor S, Mozzon M, Foligni R, Canonico L, Ciani M, Aquilanti L.   +11 more
europepmc   +1 more source

Biosorption Potential of Phanerochaete chrysosporium for Arsenic, Cadmium, and Chromium Removal from Aqueous Solutions. [PDF]

Glob Chall, 2018
Rudakiya DM, Iyer V, Shah D, Gupte A, Nath K.   +4 more
europepmc   +1 more source

Robust and cost-saving static solid cultivation method for lipid production using the chlamydospores of Phanerochaete chrysosporium. [PDF]

Biotechnol Biofuels, 2019
Liu L, Song J, Li Y, Li P, Wang H.
europepmc   +1 more source

In silico-designed lignin peroxidase from Phanerochaete chrysosporium shows enhanced acid stability for depolymerization of lignin. [PDF]

Biotechnol Biofuels, 2018
Pham LTM, Seo H, Kim KJ, Kim YH.
europepmc   +1 more source

Structural basis for oxidative decarboxylation of lignin-derived aromatics by the fungal flavoprotein monooxygenase PcMNX1. [PDF]

J Biol Chem
Mori R, Suzuki H, Ishida T, Sakai K, Yamaguchi S, Sunagawa N, Igarashi K, Kato M, Shimizu M.   +8 more
europepmc   +1 more source

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Metabolism of cyanide by Phanerochaete chrysosporium

Archives of Biochemistry and Biophysics, 1991
The oxidation of veratryl alcohol (3,4-dimethoxybenzyl alcohol) by lignin peroxidase H2 (LiP H2) from the white rot fungus Phanerochaete chrysosporium was strongly inhibited by sodium cyanide. The I50 was estimated to be about 2-3 microM. In contrast, sodium cyanide binds to the native enzyme with an apparent sodium cyanide dissociation constant Kd of ...
M M, Shah, T A, Grover, S D, Aust
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Lignin-Degrading Peroxidases from Phanerochaete chrysosporium

Journal of Biotechnology, 1990
Lignin and manganese peroxidases are secreted by the basidiomycete Phanerochaete chrysosporium during secondary metabolism. These enzymes play major roles in lignin degradation. The active site amino acid sequence of these lignin-degrading peroxidases is similar to that of horseradish peroxidase (HRP) and cytochrome c peroxidase (CcP). The mechanism by
D, Cai, M, Tien
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Two glucuronoyl esterases of Phanerochaete chrysosporium

Archives of Microbiology, 2008
The white-rot fungus Phanerochaete chrysosporium produces glucuronoyl esterase, a recently discovered carbohydrate esterase, during growth on sugar beet pulp. Two putative genes encoding this enzyme, ge1 and ge2, were isolated and cloned. Heterologous expression in Aspergillus vadensis, Pycnoporus cinnabarinus and Schizophyllum commune resulted in ...
Duranová, M., Spániková, S., Wösten, H.A.B., Biely, P., de Vries, R.P.   +4 more
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Glucose oxidase of Phanerochaete chrysosporium

1988
Publisher Summary Glucose oxidase catalyzes the oxidation of D-glucose to δ-D-gluconolactone and H 2 O 2 in the presence of molecular oxygen. In a subsequent step δ -D-gluconolactone is nonenzymatically hydrolyzed to D-gluconic acid. This enzyme has been demonstrated in various Aspergillus and Penicillium species and has recently been purified ...
R L, Kelley, C A, Reddy
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