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Kenneth E. Hammel

Researcher at University of Wisconsin-Madison

Publications -  92
Citations -  9641

Kenneth E. Hammel is an academic researcher from University of Wisconsin-Madison. The author has contributed to research in topics: Lignin & Phanerochaete. The author has an hindex of 53, co-authored 91 publications receiving 9016 citations. Previous affiliations of Kenneth E. Hammel include United States Forest Service & University of California, Berkeley.

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Genome, transcriptome, and secretome analysis of wood decay fungus Postia placenta supports unique mechanisms of lignocellulose conversion

TL;DR: Comparisons with the closely relatedwhite-rot fungus Phanerochaete chrysosporium support an evolutionary shift from white-rot to brown-rot during which the capacity for efficient depolymerization of lignin was lost.
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Oxidation of polycyclic aromatic hydrocarbons and dibenzo[p]-dioxins by Phanerochaete chrysosporium ligninase.

TL;DR: It is reported that this enzyme also catalyzes the oxidation of certain aromatic pollutants and compounds related to them, including polycyclic aromatic hydrocarbons with ionization potentials less than or equal to approximately 7.55 eV.
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Reactive oxygen species as agents of wood decay by fungi

TL;DR: Although many wood decay basidiomycetes secrete oxidative and hydrolytic enzymes that participate in lignocellulose biodedgradation, it is generally recognized now that these enzymes cannot penetrate sound wood, and that fungi must employ smaller agents to initiate decay.
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Role of fungal peroxidases in biological ligninolysis

TL;DR: Progress in the dissolution and NMR spectroscopy of plant cell walls may allow new inferences about the nature of the oxidants involved, and increasing knowledge about the genomes of ligninolytic fungi may help decide whether any of the peroxidases has an essential role.
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Comparison of lignin peroxidase, horseradish peroxidase and laccase in the oxidation of methoxybenzenes.

TL;DR: The present study investigated the possibility that other peroxidative and oxidative enzymes known to catalyse one-electron oxidations may also oxidize non-phenolics to cation-radical intermediates and that this ability is related to the redox potential of the substrate.