Results 221 to 230 of about 26,797 (254)
Some of the next articles are maybe not open access.
Improvements in the determination of manganese peroxidase activity
Biotechnology Letters, 2001The existing method of determining the activity of manganese peroxidase (MnP), produced by Phanerochaete chrysosporium, was improved. 2,6-Dimethoxyphenol at 80 mM was used as a substrate and, after the decolorization of the reaction mixture, H2O2 was added and the initial reaction rate was used to determine MnP activity.
I. Grgič +3 more
openaire +1 more source
Biochemistry, 1993
The 1H NMR spectroscopy was used to study lignin peroxidase (LiP) and manganese peroxidase (MnP) containing deuterated histidines. LiP and MnP were obtained from a histidine auxotroph of the fungus Phanerochaete chrysosporium grown in the presence of deuterated histidines. The derivatives with deuterated histidines have allowed a firm assignment of the
BANCI, LUCIA +5 more
openaire +3 more sources
The 1H NMR spectroscopy was used to study lignin peroxidase (LiP) and manganese peroxidase (MnP) containing deuterated histidines. LiP and MnP were obtained from a histidine auxotroph of the fungus Phanerochaete chrysosporium grown in the presence of deuterated histidines. The derivatives with deuterated histidines have allowed a firm assignment of the
BANCI, LUCIA +5 more
openaire +3 more sources
Resonance Raman spectroscopy of cytochrome c peroxidase variants that mimic manganese peroxidase
JBIC Journal of Biological Inorganic Chemistry, 2003Cytochrome c peroxidase (C cP) variants with an engineered Mn(II) binding site, including MnC cP [C cP(MI, G41E, V45E, H181D)], MnC cP(W191F), and MnC cP(W191F, W51F), that mimic manganese peroxidase (MnP), have been characterized by resonance Raman (RR) spectroscopy.
Manliang, Feng +5 more
openaire +2 more sources
Manganese peroxidase from Phanerochaete chrysosporium
1988Publisher Summary Manganese peroxidase is an extracellular enzyme expressed during secondary metabolism as part of the lignin-degradative system of Phanerochaete chrysosporium. This chapter discusses purification procedure of manganese peroxidase. Manganese peroxidase can be isolated from any wild-type strain of P. chrysosporium.
Michael H. Gold, Jeffrey K. Glenn
openaire +1 more source
Manganese peroxidase of Phanerochaete chrysosporium: Purification
1988Publisher Summary This chapter discusses a method for purification of the manganese peroxidase of P. chrysosporium. It discusses assay methods for manganese. Manganese peroxidase may be assayed using a variety of aromatic substrates, particularly those that are employed for assays of common peroxidascs such as horseradish peroxidase.
Andrzej Paszczyński +2 more
openaire +1 more source
Gene, 1994
Two heme proteins, manganese peroxidase (MnP) and lignin peroxidase (LiP), play key roles in the fungal depolymerization of lignin. Many cDNA and genomic clones encoding these peroxidases have been published. We report here on the cDNA lambda MP-2 encoding the MnP isozyme H3 from Phanerochaete chrysosporium strain BKM-F-1767.
A B, Orth +3 more
openaire +2 more sources
Two heme proteins, manganese peroxidase (MnP) and lignin peroxidase (LiP), play key roles in the fungal depolymerization of lignin. Many cDNA and genomic clones encoding these peroxidases have been published. We report here on the cDNA lambda MP-2 encoding the MnP isozyme H3 from Phanerochaete chrysosporium strain BKM-F-1767.
A B, Orth +3 more
openaire +2 more sources
Conversion of adamsite (phenarsarzin chloride) by fungal manganese peroxidase
Applied Microbiology and Biotechnology, 2003Fungal manganese peroxidase was found to convert the persistent chemical warfare agent adamsite (phenarsarzin chloride) in a cell-free reaction mixture containing sodium malonate, Mn(2+) ions, and reduced glutathione. The organo-arsenical compound disappeared completely within 48 h accompanied by the formation of a more polar metabolite with a clearly ...
R, Haas +5 more
openaire +2 more sources
The Effects of Calcium on the Thermal Stability and Activity of Manganese Peroxidase
Archives of Biochemistry and Biophysics, 1996The presence of micromolar Ca2+ efficiently prevented the thermal inactivation of manganese peroxidase from Phanerochaete chrysosporium. The amount of Ca2+ normally present in the enzyme decreased when the enzyme was thermally inactivated and EGTA increased the rate of inactivation.
G R, Sutherland, S D, Aust
openaire +2 more sources
Folia Microbiologica, 1994
Growth temperature played an important role in the appearance, maximum level and ratio of manganese peroxidase (MnP) and lignin peroxidase (LIP) activities in the cultures ofPhanerochaete chrysosporium. While at higher temperatures (39, 33, and 28°C) both enzymes were produced (with LIP being the major one) at 23°C MnP was dominant. At 18°C, of the two
B. R. M. Vyas, J. Volc, V. Šašek
openaire +1 more source
Growth temperature played an important role in the appearance, maximum level and ratio of manganese peroxidase (MnP) and lignin peroxidase (LIP) activities in the cultures ofPhanerochaete chrysosporium. While at higher temperatures (39, 33, and 28°C) both enzymes were produced (with LIP being the major one) at 23°C MnP was dominant. At 18°C, of the two
B. R. M. Vyas, J. Volc, V. Šašek
openaire +1 more source