Structure of Thermobifida fusca DyP-type peroxidase and activity towards Kraft lignin and lignin model compounds
نویسندگان
چکیده
منابع مشابه
Lignin peroxidase structure and function.
Lignin peroxidase (LiP) plays a central role in the biodegradation of the plant cell wall constituent lignin. LiP is able to oxidize aromatic compounds with redox potentials higher than 1.4 V (NHE) by single electron abstraction, but the exact redox mechanism is still poorly understood. The finding in our laboratory that the Cbeta-atom of Trp171 carries a unique modification led us to initiate ...
متن کاملCrystal structure of lignin peroxidase.
The crystal structure of lignin peroxidase (LiP) from the basidiomycete Phanerochaete chrysosporium has been determined to 2.6 A resolution by usine multiple isomorphous replacement methods and simulated annealing refinement. Of the 343 residues, residues 3-335 have been accounted for in the electron density map, including four disulfide bonds. The overall three-dimensional structure is very si...
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Laccase-catalyzed oxygen delignification of kraft pulp offers some potential as a replacement for conventional chemical bleaching and has the advantage of requiring much lower pressure and temperature. However, chemical mediators are required for effective delignification by laccase, and their price is currently too high at the dosages required. To date, most studies have employed laccase from ...
متن کاملAntioxidant activity of lignin phenolic compounds extracted from kraft and sulphite black liquors.
The antioxidant activity of the phenolic compounds present in industrial black liquors obtained from the two cooking processes (kraft and sulphite) used in Portugal to produce Eucalyptus globulus pulp was evaluated. The black liquors treated at several pH values were extracted with ethyl acetate. Phenolic fractions were further separated by liquid chromatography of the crude extracts of kraft l...
متن کاملDirect interaction of lignin and lignin peroxidase from Phanerochaete chrysosporium.
Binding properties of lignin peroxidase (LiP) from the basidiomycete Phanerochaete chrysosporium against a synthetic lignin (dehydrogenated polymerizate, DHP) were studied with a resonant mirror biosensor. Among several ligninolytic enzymes, only LiP specifically binds to DHP. Kinetic analysis revealed that the binding was reversible, and that the dissociation equilibrium constant was 330 micro...
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ژورنال
عنوان ژورنال: Archives of Biochemistry and Biophysics
سال: 2016
ISSN: 0003-9861
DOI: 10.1016/j.abb.2016.02.019