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Extraction of manganese peroxidase produced by Lentinula edodes

Bioresource Technology, 2008
Lentinula edodes, commonly called shiitake, is considered a choice edible mushroom with exotic taste and medicinal quality. L. edodes grows very well and produces a range of enzymes when cultivated on eucalyptus residues. Development of appropriate experimental procedures for recovery and determination of enzymes became a widely important cash crop. In
Adriane Milagres
exaly   +3 more sources

Oxidation of methoxybenzenes by manganese peroxidase and by Mn3+

Archives of Biochemistry and Biophysics, 1991
Manganese peroxidase, produced by some white-rot fungi during lignin degradation, catalyzes the oxidation of Mn2+ to Mn3+. Whereas Mn3+ is known to oxidize phenolic compounds, its role in lignin degradation is not clear. We have used a series of methoxybenzenes with E1/2 values of 1.76-0.81 V (vs saturated calomel electrode) to investigate the ...
J L, Popp, T K, Kirk
openaire   +2 more sources

Conversion of aminonitrotoluenes by fungal manganese peroxidase

Journal of Basic Microbiology, 1998
Preparations of extracellular manganese peroxidase from the white-rot fungus Nematoloma frowardii and the litter decaying fungus Stropharia rugosoannulata converted rapidly the main intermediates of the explosive 2,4,-trinitrotoluene--the aminonitrotoluenes. In a cell-free system, 2-amino-4,6-dinitrotoluene, 4-amino-2,6-dinitrotoluene and 2,6-diamino-4-
K, Scheibner, M, Hofrichter
openaire   +2 more sources

Monitoring the Role of Oxalate in Manganese Peroxidase

Biochemistry, 1998
The water proton relaxation rate measurements between 0.01 and 50 MHz on water solutions containing the cyanide adduct of the manganese-depleted manganese peroxidase (MnP-CN-) and increasing amounts of Mn2+ have been determined. The proton relaxivity curves have shown evidence of the formation of the protein/Mn2+ complex and have been analyzed in order
L, Banci   +4 more
openaire   +2 more sources

Substrate Specificity of Lignin Peroxidase and a S168W Variant of Manganese Peroxidase

Archives of Biochemistry and Biophysics, 2000
Lignin peroxidase (LiP) and manganese peroxidase (MnP) are structurally similar heme-containing enzymes secreted by white-rot fungi. Unlike MnP, which is only specific for Mn(2+), LiP has broad substrate specificity, but it is not known if this versatility is due to multiple substrate-binding sites.
S L, Timofeevski   +3 more
openaire   +2 more sources

Characterization of Manganese(II) Binding Site Mutants of Manganese Peroxidase

Biochemistry, 1996
A series of site-directed mutants, E35Q, E39Q, and E35Q-D179N, in the gene encoding manganese peroxidase isozyme 1 (mnp1) from Phanerochaete chrysosporium, was created by overlap extension, using the polymerase chain reaction. The mutant genes were expressed in P.
K, Kishi   +5 more
openaire   +2 more sources

High-yield production of manganese peroxidase, lignin peroxidase, and versatile peroxidase in Phanerochaete chrysosporium

Applied Microbiology and Biotechnology, 2014
The white-rot fungus Phanerochaete chrysosporium secretes extracellular oxidative enzymes during secondary metabolism, but lacks versatile peroxidase, an enzyme important in ligninolysis and diverse biotechnology processes. In this study, we report the genetic modification of a P.
Nancy, Coconi-Linares   +5 more
openaire   +2 more sources

Redesign of Cytochrome c Peroxidase into a Manganese Peroxidase:  Role of Tryptophans in Peroxidase Activity

Biochemistry, 1999
Trp191Phe and Trp51Phe mutations have been introduced into an engineered cytochrome c peroxidase (CcP) containing a Mn(II)-binding site reported previously (MnCcP; see Yeung, B. K.-S., et al. (1997) Chem. Biol. 5, 215-221). The goal of the present study is to elucidate the role of tryptophans in peroxidase activity since CcP contains both Trp51 and ...
A, Gengenbach, S, Syn, X, Wang, Y, Lu
openaire   +2 more sources

Fungal laccase, manganese peroxidase and lignin peroxidase: Gene expression and regulation

Enzyme and Microbial Technology, 2013
Extensive research efforts have been dedicated to characterizing expression of laccases and peroxidases and their regulation in numerous fungal species. Much attention has been brought to these enzymes broad substrate specificity resulting in oxidation of a variety of organic compounds which brings about possibilities of their utilization in ...
Grzegorz Janusz   +4 more
openaire   +2 more sources

Studies on the Properties and Co-immobilization of Manganese Peroxidase

Chinese Journal of Biotechnology, 2007
White-rot fungus manganese peroxidase (MnP) oxidizes a wide range of substrates, rendering it an interesting enzyme for potential applications. The stability of MnP can be improved by immobilization. With sodium alginate, gelatin, or chitosan as a carrier, and glutaraldehyde as the crosslinking agent, MnP was co-immobilized using the embed-crosslinked ...
Xiao-Bin, Cheng   +5 more
openaire   +2 more sources

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