Topic
Lignin peroxidase
About: Lignin peroxidase is a research topic. Over the lifetime, 1707 publications have been published within this topic receiving 84177 citations. The topic is also known as: diarylpropane oxygenase & diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving).
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TL;DR: This paper presents a meta-analyses of IGNIN as a stimulus and its applications in medicine and physiology, and discusses the role that IGNIN plays in the development of disease and its role in medicine.
Abstract: INTRODUCTION ....................................................................................................................................... 465 LIGNIN AS A SUBSTRATE ............................................................................................................................... 466 MICROBIOLOGY OF LIGNIN BIODEGRADATI ON ........................................................................... 468 Anaerobic Conditions ............................................................................................................................... 469 Aerobic Conditions ................................................................................................................................... 469 LIGNIN DEGRADATION BY WHITEROT FUNGI ............................................................................. 471 Physiology .......................................................................................................................................................... 472 Biochemistry ............................................................................................................................................ 475 Genetics ..............................................................................................................................................................486 Molecular Biology .................................................................................................................................... 489 CONCLUSIONS AND RECOMMENDATIONS ..................................................................................... 491 ENZYMATIC “COMBUSTION” ........................................................................................................................ 493
2,556 citations
TL;DR: The biodegradation of PAHs has been observed under both aerobic and anaerobic conditions and the rate can be enhanced by physical/chemical pretreatment of contaminated soil.
2,482 citations
TL;DR: An extracellular lignin-degrading enzyme from the basidiomycete Phanerochaete chrysosporium Burdsall was purified to homogeneity by ion-exchange chromatography, finding that it is an oxygenase, unique in its requirement for H(2)O(2).
Abstract: An extracellular lignin-degrading enzyme from the basidiomycete Phanerochaete chrysosporium Burdsall was purified to homogeneity by ion-exchange chromatography. The 42,000-dalton ligninase contains one protoheme IX per molecule. It catalyzes, nonstereospecifically, several oxidations in the alkyl side chains of lignin-related compounds: Cα—Cβ cleavage in lignin-related compounds of the type aryl—CαHOH—CβHR—CγH2OH (R = -aryl or -O-aryl), oxidation of benzyl alcohols to aldehydes or ketones, intradiol cleavage in phenylglycol structures, and hydroxylation of benzylic methylene groups. It also catalyzes oxidative coupling of phenols, perhaps explaining the long-recognized association between phenol oxidation and lignin degradation. All reactions require H2O2. The Cα—Cβ cleavage and methylene hydroxylation reactions involve substrate oxygenation; the oxygen atom is from O2 and not H2O2. Thus the enzyme is an oxygenase, unique in its requirement for H2O2.
1,258 citations
TL;DR: The extracellular fluid of ligninolytic cultures of the wood-decomposing basidiomycete Phanerochaete chrysosporium Burds contains an enzyme that degrades lignin substructure model compounds as well as spruce and birch lignins.
Abstract: The extracellular fluid of ligninolytic cultures of the wood-decomposing basidiomycete Phanerochaete chrysosporium Burds. contains an enzyme that degrades lignin substructure model compounds as well as spruce and birch lignins. It has a molecular size of 42,000 daltons and requires hydrogen peroxide for activity.
1,230 citations
TL;DR: The most efficient lignin degraders, estimated by 14CO2 evolution from 14C-[Ring]-labelled synthetic lign in (DHP), belong to the first group, whereas many of the most selective lignIn-degrading fungi belong toThe second, although only moderate to good [14C]DHP mineralization is obtained using fungi from this group.
Abstract: White-rot fungi produce extracellular lignin-modifying enzymes, the best characterized of which are laccase (EC 1.10.3.2), lignin peroxidases (EC 1.11.1.7) and manganese peroxidases (EC 1.11.1.7). Lignin biodegradation studies have been carried out mostly using the white-rot fungus Phanerochaete chrysosporium which produces multiple isoenzymes of lignin peroxidase and manganese peroxidase but does not produce laccase. Many other white-rot fungi produce laccase in addition to lignin and manganese peroxidases and in varying combinations. Based on the enzyme production patterns of an array of white-rot fungi, three categories of fungi are suggested: (i) lignin-manganese peroxidase group (e.g.P. chrysosporium and Phlebia radiata), (ii) manganese peroxidase-laccase group (e.g. Dichomitus squalens and Rigidoporus lignosus), and (iii) lignin peroxidase-laccase group (e.g. Phlebia ochraceofulva and Junghuhnia separabilima). The most efficient lignin degraders, estimated by 14CO2 evolution from 14C-[Ring]-labelled synthetic lignin (DHP), belong to the first group, whereas many of the most selective lignin-degrading fungi belong to the second, although only moderate to good [14C]DHP mineralization is obtained using fungi from this group. The lignin peroxidase-laccase fungi only poorly degrade [14C]DHP.
1,112 citations