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Mechanism of aromatic ring cleavage of β-O-4 lignin substructure models by lignin peroxidase [PDF]

FEBS Letters, 1987
This investigation examined the aromatic ring cleavage of β-O-4 lignin substructure model compounds by lignin peroxidase of Phanerochaete chrysosporium. Based on tracer experiments using H218O and 18O2, mechanisms of the aromatic ring cleavage of the β-O-
Toshiaki Umezawa
exaly   +2 more sources

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Incorporation of peroxidase into synthetic lignin

Journal of Agricultural and Food Chemistry, 1991
A synthetic lignin was produced by using coniferyl alcohol, horseradish peroxidase, and H2O2. The lignin contained 9.4% protein which was contributed by the peroxidase, probably by cross-linking of the tyrosine residues from the protein to the monomeric or polymeric intermediates during the reaction (.)
John J. Evans, David S. Himmelsbach
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Characterization of lignin peroxidase-encoding genes from lignin-degrading basidiomycetes

Gene, 1990
Two closely linked lignin peroxidase (LPO)-encoding genes (lpo) from Phanerochaete chrysosporium were isolated. Nucleotide sequence studies indicated that the two genes are separated by 1.3 kb of flanking DNA and transcribed in opposite directions. Cloned P. chrysosporium lpo gene probes have been shown to hybridize to multiple sequences present in the
K, Huoponen, P, Ollikka, M, Kälin, I, Walther, P, Mäntsälä, J, Reiser   +5 more
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Lignin peroxidase of Phanerochaete chrysosporium

1988
Publisher Summary Several procedures have been described for growing Phanerochaete chrysosporiurn for ligninase production. These procedures differ somewhat in the medium formulation and types of growth vessels: (1) shallow stationary cultures, (2) agitated liquid cultures, and (3) rotating biological contactors (RBCs; disk fermenters).
Ming Tien, T.Kent Kirk
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Inhibition of lignin peroxidase H2 by sodium azide

Archives of Biochemistry and Biophysics, 1991
The oxidation of veratryl alcohol (3,4-dimethoxybenzyl alcohol) by lignin peroxidase H2 from Phanerochaete chrysosporium and H2O2 was strongly inhibited by sodium azide. Inhibition was competitive with respect to veratryl alcohol (Ki = 1-2 microM) and uncompetitive with respect to H2O2.
H, Tuisel, T A, Grover, J R, Lancaster, J A, Bumpus, S D, Aust   +4 more
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Inactivation of lignin peroxidase by phenylhydrazine and sodium azide

Archives of Biochemistry and Biophysics, 1990
Lignin peroxidase (LiP) is rapidly inactivated in a concentration-dependent manner by H2O2 and either phenylhydrazine or sodium azide. Full inactivation of isozyme 2b (H8) requires approximately 50 eq of phenylhydrazine or 80 eq of sodium azide. Anaerobic incubation of isozyme 2b with [14C]phenylhydrazine and H2O2 results in 77% loss of catalytic ...
G D, DePillis, H, Wariishi, M H, Gold, P R, Ortiz de Montellano   +3 more
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The Effect of Manganese on the Oxidation of Chemicals by Lignin Peroxidase

Biochemistry, 1995
It has recently been discovered that lignin peroxidase isozyme H2 (LiPH2) has the ability to oxidize Mn2+ (Khindaria et al., 1995). Furthermore, at pH 4.5, the physiological pH of Phanerochaete chrysosporium, LiPH2 oxidizes Mn2+ at a much faster rate (25 times) than veratryl alcohol (VA).
G R, Sutherland, A, Khindaria, N, Chung, S D, Aust   +3 more
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Lignin peroxidases can also oxidize manganese

Biochemistry, 1995
The peroxidase isozymes secreted by the white rot fungus Phanerochaete chrysosporium include lignin peroxidases and manganese-dependent peroxidases. The major isozymes, called lignin peroxidases, are thought to oxidize chemicals directly. The manganese-dependent peroxidases (H3, H4, H5, and H9) are relatively minor, making up only a fraction of the ...
A, Khindaria, D P, Barr, S D, Aust
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Electroenzymatic oxidation of veratryl alcohol by lignin peroxidase

Journal of Biotechnology, 2003
This paper reports the formation of veratraldehyde by electroenzymatic oxidation of veratryl alcohol (3,4-dimethoxybenzyl alcohol) hybridizing both electrochemical and enzymatic reactions and using lignin peroxidase. The novel electroenzymatic method was found to be effective for replacement of hydrogen peroxide by an electrochemical reactor, which is ...
KiBeom, Lee, Seung-Hyeon, Moon
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Display of Lignin Peroxidase on the Surface of Bacillus subtilis

Applied Biochemistry and Biotechnology
Lignin peroxidase (LiP) has a good application prospect in lignin degradation, environmental treatment, straw feed, and other industries. However, its application is constrained by the high price and low stability of enzyme preparation. In this study, the Escherichia coli-Bacillus subtilis (E. coli-B.
Shouzhi Li, Lu He, Na Shi, Zhong Ni, Quan Bu, Daochen Zhu, Huayou Chen   +6 more
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