Results 201 to 210 of about 198,237 (244)
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Applied Biochemistry and Biotechnology, 1998
The abilities of lignin peroxidase (LIP) and manganese peroxidase (MNP) from Phanerochaete chrysosporium to degrade an insoluble hardwood lignin in vitro in aqueous media were tested. Neither LIP nor MNP appreciably changed the mass or lignin content, although both produced small amounts of unique solubilized lignin fragments.
D N, Thompson +3 more
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The abilities of lignin peroxidase (LIP) and manganese peroxidase (MNP) from Phanerochaete chrysosporium to degrade an insoluble hardwood lignin in vitro in aqueous media were tested. Neither LIP nor MNP appreciably changed the mass or lignin content, although both produced small amounts of unique solubilized lignin fragments.
D N, Thompson +3 more
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The substrate binding sites of lignin peroxidase and manganese peroxidase [PDF]
, 2002 The lignin-degrading fungus, Phanerochaete chrysosporium, secretes two families of extracellular peroxidases, lignin peroxidase (Lip) and manganese peroxidase (MnP), which are major enzymatic components of its extracellular lignin degradation ...
Gelpke, Maarten
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Lignin-Degrading Peroxidases from Phanerochaete chrysosporium
Journal of Biotechnology, 1990Lignin 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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Lignin and Mn Peroxidase-Catalyzed Oxidation of Phenolic Lignin Oligomers
Biochemistry, 1999The oxidation of phenolic oligomers by lignin and manganese peroxidases was studied by transient-state kinetic methods. The reactivity of peroxidase intermediates compound I and compound II was studied with the phenol guaiacol along with a beta-O-4 phenolic dimer, trimer, and tetramer.
BANCI, LUCIA +2 more
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Veratryl alcohol oxidation by lignin peroxidase
Biochemistry, 1995Lignin peroxidase (LiP) from the white rot fungus Phanerochaete chrysosporium catalyzes the H2O2-dependent oxidation of veratryl alcohol (VA), a secondary metabolite of the fungus, to veratryl aldehyde (VAD). The oxidation of VA does not seem to be simply one-electron oxidation by LiP compound I (LiPI) to its cation radical (VA.+) and the second by LiP
A, Khindaria, I, Yamazaki, S D, Aust
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Oxidation of Ferrocytochrome c by Lignin Peroxidase
Biochemistry, 1994We demonstrate direct oxidation of ferrocytochrome c by lignin peroxidase (LiP) from the lignin-degrading basidiomycete, Phanerochaete chrysosporium. Steady-state kinetic data fit a peroxidase ping-pong mechanism rather than an ordered bi-bi ping-pong mechanism, suggesting that the reductions of LiP compounds I and II by ferrocytochrome c are ...
H, Wariishi, D, Sheng, M H, Gold
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Catalytic mechanisms and regulation of lignin peroxidase
Biochemical Society Transactions, 1992Lignin peroxidase (LiP) is a fungal haemoprotein similar to the lignin-synthesizing plant peroxidases, but it has a higher oxidation potential and oxidizes dimethoxylated aromatic compounds to radical cations. It catalyses the degradation of lignin models but in vitro the outcome is net lignin polymerization.
P J, Harvey +5 more
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Metallophthalocyanines as possible lignin peroxidase models
Bioorganic & Medicinal Chemistry, 1995Several metalloporphyrins, particularly highly chlorinated water soluble meso-tetraphenylporphyrins, have been shown to be good biomimetics of the lignin peroxidases which degrade lignin in vivo. Metal complexes of the water soluble phthalocyaninetetrasulfonic acid have been examined as catalysts for the oxidation of lignin since the phthalocyanines ...
F, Cui, D, Dolphin
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Lignin peroxidase-type activity of soybean peroxidase
Enzyme and Microbial Technology, 1995Soybean peroxidase (SBP), an acidic peroxidase isolated from the hulls of the bean, catalyzes the efficient oxidation of veratryl alcohol to veratraldehyde in the presence of H2O2. The reaction is optimal at pH 2.4 in the presence of 0.2 m CaCl2. Soybean peroxidase is highly thermostable at pH 2.4, with half-lives of 210 and 2.5 h at 30 and 50°C ...
James P. McEldoon +2 more
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Substrate Specificity of Lignin Peroxidase and a S168W Variant of Manganese Peroxidase
Archives of Biochemistry and Biophysics, 2000Lignin 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
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