Reaction kinetics of versatile peroxidase for the degradation of lignin compounds

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dc.contributor.author Busse, N.
dc.contributor.author Wagner, D.
dc.contributor.author Kraume, M.
dc.contributor.author Czermak, Peter
dc.date.accessioned 2013-10-03T20:44:29Z
dc.date.available 2013-10-03T20:44:29Z
dc.date.issued 2013-10-03
dc.identifier.uri http://hdl.handle.net/2097/16602
dc.description.abstract The H[subscript 2]O[subscript 2] dependent degradation of adlerol by a crude versatile peroxidase from Bjekandera adusta, a new ligninolytic enzyme, was investigated. Adlerol (1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)-1,3-propanediol)) is a non phenolic β-O-4 dimer whose structural architecture represents the most abundant unit (50-65%) of the valuable renewable biopolymer lignin. Lignin removel plays a key role in utilizing lignocellulosic biomass in biorefineries. Steady state analyses in the µL scale showed saturation kinetics for both, H[subscript 2]O[subscript 2] and adlerol with quite sensitive response to H[subscript 2]O[subscript 2]. This was characterized through slow transient states (lag phases) prior steady state and were enhanced by increasing H[subscript 2]O[subscript 2] concentration. The major reason for such phenomena was found to be an accumulation of compound III (E[superscript III]) via reaction of compound II (E[superscript II]) with H[subscript 2]O[subscript 2]; instead with adlerol to the enzymeâ s ground state E[superscript 0] in order to restart another catalytic cycle. As result, the enzyme deviated from its normal catalytic cycle. A corresponding threshold was determined at ≥ 50 μM H[subscript 2]O[subscript 2] and an adlerol to H[subscript 2]O[subscript 2] ratio of 15:1 for the given conditions. Furthermore, E[superscript III] did not represent a catalytical dead end intermediate as it is generally described. By an additional decrease of the adlerol to H[subscript 2]O[subscript 2] ratio of ca. 3 at the latest, considerable irreversible enzyme deactivations occurred promoted through reaction of E[superscript III] with H[subscript 2]O[subscript 2]. At a mL scale deactivation kinetics by H[subscript 2]O[subscript 2] were further examined in dependence on adlerol presence. The course followed a time dependent irreversible deactivation (two step mechanism) and was diminished in the presence of adlerol. The deactivation could be sufficiently described by an equation similar to the Michaelis Menten type, competitive inhibited by adlerol. Finally, first estimates of the kinetic parameters v[subscript max], K[subscript m][superscript S1] (S[subscript 1]: H[subscript 2]O[subscript 2]), K[subscript m][superscript S2] (S[subscript 2]: adlerol), k[subscript i][superscript app] and K[subscript i][superscript app] were made. Moreover, the peroxidase reaction mechanism was reviewed and recommendations are given preventing permature enzyme losses. en_US
dc.language.iso en_US en_US
dc.relation.uri http://thescipub.com/abstract/10.3844/ajbbsp.2013.365.394 en_US
dc.subject Versatile peroxidase en_US
dc.subject Lignin model compound en_US
dc.subject Steady-state kinetics en_US
dc.subject Slow transient states en_US
dc.subject Deactivation en_US
dc.title Reaction kinetics of versatile peroxidase for the degradation of lignin compounds en_US
dc.type Article (publisher version) en_US
dc.date.published 2013 en_US
dc.citation.doi doi:10.3844/ajbbsp.2013.365.394 en_US
dc.citation.epage 394 en_US
dc.citation.issue 4 en_US
dc.citation.jtitle American Journal of Biochemistry and Biotechnology en_US
dc.citation.spage 365 en_US
dc.citation.volume 9 en_US
dc.contributor.authoreid pczermak en_US


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