Expanding the scope of laccase-mediator systems

Research output: Contribution to journalArticleResearchpeer review

Authors

  • Paul Könst
  • Selin Kara
  • Svenja Kochius
  • Dirk Holtmann
  • Isabel W.C.E. Arends
  • Roland Ludwig
  • Frank Hollmann

External Research Organisations

  • Delft University of Technology
  • DECHEMA E.V., Karl-Winnacker-Institut
  • University of Natural Resources and Applied Life Sciences (BOKU)
View graph of relations

Details

Original languageEnglish
Pages (from-to)3027-3032
Number of pages6
JournalCHEMCATCHEM
Volume5
Issue number10
Early online date3 Jul 2013
Publication statusPublished - Oct 2013
Externally publishedYes

Abstract

The laccase-mediator system (LMS) for the regeneration of oxidised nicotinamide co-factors was revisited to broaden the mediator scope. Among the 18 mediators screened, acetosyringone, syringaldehyde and caffeic acid excelled with respect to activity and stability under process conditions. The LMS based on the laccase from Myceliophthora thermophila and acetosyringone was further investigated and applied to promote the nicotinamide adenine dinucleotide (NAD+)-dependent oxidation of glucose as well as the oxidative lactonisation of 1,4-butanediol to the corresponding γ-butyrolactone. Laccase gets a look-in: The laccase-mediator system (LMS) for the regeneration of oxidized nicotinamide co-factors is revisited to broaden the mediator scope. The LMS based on the laccase from Myceliophthora thermophila and acetosyringone is applied to promote the oxidation of glucose and the oxidative lactonization of 1,4-butanediol to the corresponding γ-butyrolactone.

Keywords

    Biocatalysis, Cofactors, Enzyme catalysis, Lactones, Oxidation

ASJC Scopus subject areas

Cite this

Expanding the scope of laccase-mediator systems. / Könst, Paul; Kara, Selin; Kochius, Svenja et al.
In: CHEMCATCHEM, Vol. 5, No. 10, 10.2013, p. 3027-3032.

Research output: Contribution to journalArticleResearchpeer review

Könst, P, Kara, S, Kochius, S, Holtmann, D, Arends, IWCE, Ludwig, R & Hollmann, F 2013, 'Expanding the scope of laccase-mediator systems', CHEMCATCHEM, vol. 5, no. 10, pp. 3027-3032. https://doi.org/10.1002/cctc.201300205
Könst, P., Kara, S., Kochius, S., Holtmann, D., Arends, I. W. C. E., Ludwig, R., & Hollmann, F. (2013). Expanding the scope of laccase-mediator systems. CHEMCATCHEM, 5(10), 3027-3032. https://doi.org/10.1002/cctc.201300205
Könst P, Kara S, Kochius S, Holtmann D, Arends IWCE, Ludwig R et al. Expanding the scope of laccase-mediator systems. CHEMCATCHEM. 2013 Oct;5(10):3027-3032. Epub 2013 Jul 3. doi: 10.1002/cctc.201300205
Könst, Paul ; Kara, Selin ; Kochius, Svenja et al. / Expanding the scope of laccase-mediator systems. In: CHEMCATCHEM. 2013 ; Vol. 5, No. 10. pp. 3027-3032.
Download
@article{caa2deef229344dd876217aad9e65811,
title = "Expanding the scope of laccase-mediator systems",
abstract = "The laccase-mediator system (LMS) for the regeneration of oxidised nicotinamide co-factors was revisited to broaden the mediator scope. Among the 18 mediators screened, acetosyringone, syringaldehyde and caffeic acid excelled with respect to activity and stability under process conditions. The LMS based on the laccase from Myceliophthora thermophila and acetosyringone was further investigated and applied to promote the nicotinamide adenine dinucleotide (NAD+)-dependent oxidation of glucose as well as the oxidative lactonisation of 1,4-butanediol to the corresponding γ-butyrolactone. Laccase gets a look-in: The laccase-mediator system (LMS) for the regeneration of oxidized nicotinamide co-factors is revisited to broaden the mediator scope. The LMS based on the laccase from Myceliophthora thermophila and acetosyringone is applied to promote the oxidation of glucose and the oxidative lactonization of 1,4-butanediol to the corresponding γ-butyrolactone.",
keywords = "Biocatalysis, Cofactors, Enzyme catalysis, Lactones, Oxidation",
author = "Paul K{\"o}nst and Selin Kara and Svenja Kochius and Dirk Holtmann and Arends, {Isabel W.C.E.} and Roland Ludwig and Frank Hollmann",
year = "2013",
month = oct,
doi = "10.1002/cctc.201300205",
language = "English",
volume = "5",
pages = "3027--3032",
journal = "CHEMCATCHEM",
issn = "1867-3880",
publisher = "Wiley - VCH Verlag GmbH & CO. KGaA",
number = "10",

}

Download

TY - JOUR

T1 - Expanding the scope of laccase-mediator systems

AU - Könst, Paul

AU - Kara, Selin

AU - Kochius, Svenja

AU - Holtmann, Dirk

AU - Arends, Isabel W.C.E.

AU - Ludwig, Roland

AU - Hollmann, Frank

PY - 2013/10

Y1 - 2013/10

N2 - The laccase-mediator system (LMS) for the regeneration of oxidised nicotinamide co-factors was revisited to broaden the mediator scope. Among the 18 mediators screened, acetosyringone, syringaldehyde and caffeic acid excelled with respect to activity and stability under process conditions. The LMS based on the laccase from Myceliophthora thermophila and acetosyringone was further investigated and applied to promote the nicotinamide adenine dinucleotide (NAD+)-dependent oxidation of glucose as well as the oxidative lactonisation of 1,4-butanediol to the corresponding γ-butyrolactone. Laccase gets a look-in: The laccase-mediator system (LMS) for the regeneration of oxidized nicotinamide co-factors is revisited to broaden the mediator scope. The LMS based on the laccase from Myceliophthora thermophila and acetosyringone is applied to promote the oxidation of glucose and the oxidative lactonization of 1,4-butanediol to the corresponding γ-butyrolactone.

AB - The laccase-mediator system (LMS) for the regeneration of oxidised nicotinamide co-factors was revisited to broaden the mediator scope. Among the 18 mediators screened, acetosyringone, syringaldehyde and caffeic acid excelled with respect to activity and stability under process conditions. The LMS based on the laccase from Myceliophthora thermophila and acetosyringone was further investigated and applied to promote the nicotinamide adenine dinucleotide (NAD+)-dependent oxidation of glucose as well as the oxidative lactonisation of 1,4-butanediol to the corresponding γ-butyrolactone. Laccase gets a look-in: The laccase-mediator system (LMS) for the regeneration of oxidized nicotinamide co-factors is revisited to broaden the mediator scope. The LMS based on the laccase from Myceliophthora thermophila and acetosyringone is applied to promote the oxidation of glucose and the oxidative lactonization of 1,4-butanediol to the corresponding γ-butyrolactone.

KW - Biocatalysis

KW - Cofactors

KW - Enzyme catalysis

KW - Lactones

KW - Oxidation

UR - http://www.scopus.com/inward/record.url?scp=84884947705&partnerID=8YFLogxK

U2 - 10.1002/cctc.201300205

DO - 10.1002/cctc.201300205

M3 - Article

AN - SCOPUS:84884947705

VL - 5

SP - 3027

EP - 3032

JO - CHEMCATCHEM

JF - CHEMCATCHEM

SN - 1867-3880

IS - 10

ER -

By the same author(s)