Results 161 to 170 of about 14,094 (210)

Decolourizing distillery spent wash using fungal biotechnologies: from pollution to potential. [PDF]

Bioresour Bioprocess
Singh AP, Dongre S, Sharma S, Joshi K, Bagdare H, Bobade R, Prakash O, Sharma R.   +7 more
europepmc   +1 more source

Dairy wastewater valorization enhances white rot fungi performance in recycled paper effluent treatment. [PDF]

Sci Rep
Kamali H, Gholami M, Ehrampoush MH, Nodoushan AAJ, Ghafourzadeh M, Jambarsang S, Ghaneian MT.   +6 more
europepmc   +1 more source

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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
openaire   +2 more sources

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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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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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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Phanerochaete chrysosporium Genomics

2005
A high quality draft genome sequence has been generated for the lignocellulose-degrading basidiomycete Phanerochaete chrysosporium ( Martinez et al. 2004 ). Analysis of the genome in the context of previously established genetics and physiology is presented.
Luis F. Larrondo, Rafael Vicuña, Dan Cullen   +2 more
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Chlorophenol degradation by Phanerochaete chrysosporium

Bioresource Technology, 1997
Degradation of chlorophenols by P. chrysosporium in static cultures has been studied. The influences of mycelium acclimation, co-substrate concentration and nitrogen source on phenol degradation were analyzed. With non-acclimated mycelium the maximal concentrations degraded were 150 ppm of o-chorophenol and 100 ppm of the isomers m- and p-chlorophenol.
R.Rubio Pérez, G.González Benito, M.Peña Miranda   +2 more
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Biocatalytic decolourisation of molasses by Phanerochaete chrysosporium

Bioresource Technology, 2006
Bioremediation potential of Phanerochaete chrysosporium strains NCIM 1073, NCIM 1106 and NCIM 1197 to decolourise molasses in solid and liquid molasses media was studied. Strains varied in the pattern of molasses decolourisation on solid medium by Giant colony method. Under submerged cultivation conditions, strain NCIM 1073 did not decolourise molasses
A P, Thakkar, V S, Dhamankar, B P, Kapadnis   +2 more
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Multiple ligninase-related genes from Phanerochaete chrysosporium

Gene, 1988
We have investigated four distinct sequences in genomic DNA of Phanerochaete chrysosporium that show strong homology to a lignin peroxidase cDNA sequence [Tien and Tu: Nature 236 (1987) 520-523, and 328 (1987) 742]. The complete nucleotide sequence of one of these genes is presented here.
A, Brown, P F, Sims, U, Raeder, P, Broda
openaire   +2 more sources