Reactivity of bacterial and fungal laccases with lignin under alkaline conditions

Raquel Moya, Päivi Saastamoinen, Manuel Hernández, Anna Suurnäkki, Enriqueta Arias, Maija-Liisa Mattinen (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

34 Citations (Scopus)

Abstract

The ability of Streptomyces ipomoea laccase to polymerize secoisolariciresinol lignan and technical lignins was assessed. The reactivity of S. ipomoea laccase was also compared to that of low redox fungal laccase from Melanocarpus albomyces using low molecular mass p-coumaric, ferulic and sinapic acid as well as natural (acetosyringone) and synthetic 2,2,6,6-tetramethylpiperidine 1-oxyl (TEMPO) mediators as substrates. Oxygen consumption measurement, MALDI-TOF MS and SEC were used to follow the enzymatic reactions at pH 7, 8, 9 and 10 at 30 °C and 50 °C. Polymerization of lignins and lignan by S. ipomoea laccase under alkaline reaction conditions was observed, and was enhanced in the presence of acetosyringone almost to the level obtained with M. albomyces laccase without mediator. Reactivities of the enzymes towards acetosyringone and TEMPO were similar, suggesting exploitation of the compounds and low redox laccase in lignin valorization under alkaline conditions. The results have scientific impact on basic research of laccases.
Original languageEnglish
Pages (from-to)10006-10012
JournalBioresource Technology
Volume102
Issue number21
DOIs
Publication statusPublished - 2011
MoE publication typeA1 Journal article-refereed

Keywords

  • Laccase
  • Streptomyces ipomoea
  • Melanocarpus albomyces
  • lignin
  • alkali

Fingerprint Dive into the research topics of 'Reactivity of bacterial and fungal laccases with lignin under alkaline conditions'. Together they form a unique fingerprint.

  • Cite this

    Moya, R., Saastamoinen, P., Hernández, M., Suurnäkki, A., Arias, E., & Mattinen, M-L. (2011). Reactivity of bacterial and fungal laccases with lignin under alkaline conditions. Bioresource Technology, 102(21), 10006-10012. https://doi.org/10.1016/j.biortech.2011.08.046