Modification of lignans by Trametes hirsuta laccase

Maija-Liisa Mattinen (Corresponding Author), Karin Struijs, Tapani Suortti, Ismo Mattila, Kristiina Kruus, Stefan Willför, Tarja Tamminen, Jean-Paul Vincken

Research output: Contribution to journalArticleScientificpeer-review

10 Citations (Scopus)

Abstract

Oxidative polymerization of two isolated lignans, secoisolariciresinol, and secoisolariciresinol diglucoside, as well as the lignan macromolecule, by a high redox potential Trametes hirsuta laccase was studied with different analytical methods. The reactivity of laccase with the different compounds was studied by an oxygen consumption measurement. The polymerization of laccase-treated lignans was evidenced by size exclusion chromatography, reversed phase - high performance liquid chromatography, and matrix-assisted laser desorption/ionisation - time of flight mass spectrometry. The data showed that the selected substrates could be oxidised by laccase. Secoisolariciresinol and secoisolariciresinol diglucoside were polymerized by laccase to a similar extent. The lignan macromolecule reacted to a lesser extent. Polymerization of the macromolecule proceeded mainly via its secoisolariciresinol diglucoside moieties. Furthermore, it was shown that ferulic acid can be linked to polymerized secoisolariciresinol via decarboxylation by laccase. This investigation showed that lignans can be enzymatically modified by Trametes hirsuta laccase.
Original languageEnglish
Pages (from-to)482-496
Number of pages16
JournalBioResources
Volume4
Issue number2
Publication statusPublished - 2009
MoE publication typeA1 Journal article-refereed

Fingerprint

Laccase
Lignans
Macromolecules
polymerization
Polymerization
decarboxylation
Size exclusion chromatography
High performance liquid chromatography
redox potential
ferulic acid
oxygen consumption
chromatography
Ionization
Mass spectrometry
liquid chromatography
analytical method
Desorption
desorption
ionization
mass spectrometry

Keywords

  • Lignan
  • laccase
  • polymerization
  • SEC
  • MALDI-TOF MS
  • FTIR

Cite this

Mattinen, M-L., Struijs, K., Suortti, T., Mattila, I., Kruus, K., Willför, S., ... Vincken, J-P. (2009). Modification of lignans by Trametes hirsuta laccase. BioResources, 4(2), 482-496.
Mattinen, Maija-Liisa ; Struijs, Karin ; Suortti, Tapani ; Mattila, Ismo ; Kruus, Kristiina ; Willför, Stefan ; Tamminen, Tarja ; Vincken, Jean-Paul. / Modification of lignans by Trametes hirsuta laccase. In: BioResources. 2009 ; Vol. 4, No. 2. pp. 482-496.
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Mattinen, M-L, Struijs, K, Suortti, T, Mattila, I, Kruus, K, Willför, S, Tamminen, T & Vincken, J-P 2009, 'Modification of lignans by Trametes hirsuta laccase', BioResources, vol. 4, no. 2, pp. 482-496.

Modification of lignans by Trametes hirsuta laccase. / Mattinen, Maija-Liisa (Corresponding Author); Struijs, Karin; Suortti, Tapani; Mattila, Ismo; Kruus, Kristiina; Willför, Stefan; Tamminen, Tarja; Vincken, Jean-Paul.

In: BioResources, Vol. 4, No. 2, 2009, p. 482-496.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Modification of lignans by Trametes hirsuta laccase

AU - Mattinen, Maija-Liisa

AU - Struijs, Karin

AU - Suortti, Tapani

AU - Mattila, Ismo

AU - Kruus, Kristiina

AU - Willför, Stefan

AU - Tamminen, Tarja

AU - Vincken, Jean-Paul

PY - 2009

Y1 - 2009

N2 - Oxidative polymerization of two isolated lignans, secoisolariciresinol, and secoisolariciresinol diglucoside, as well as the lignan macromolecule, by a high redox potential Trametes hirsuta laccase was studied with different analytical methods. The reactivity of laccase with the different compounds was studied by an oxygen consumption measurement. The polymerization of laccase-treated lignans was evidenced by size exclusion chromatography, reversed phase - high performance liquid chromatography, and matrix-assisted laser desorption/ionisation - time of flight mass spectrometry. The data showed that the selected substrates could be oxidised by laccase. Secoisolariciresinol and secoisolariciresinol diglucoside were polymerized by laccase to a similar extent. The lignan macromolecule reacted to a lesser extent. Polymerization of the macromolecule proceeded mainly via its secoisolariciresinol diglucoside moieties. Furthermore, it was shown that ferulic acid can be linked to polymerized secoisolariciresinol via decarboxylation by laccase. This investigation showed that lignans can be enzymatically modified by Trametes hirsuta laccase.

AB - Oxidative polymerization of two isolated lignans, secoisolariciresinol, and secoisolariciresinol diglucoside, as well as the lignan macromolecule, by a high redox potential Trametes hirsuta laccase was studied with different analytical methods. The reactivity of laccase with the different compounds was studied by an oxygen consumption measurement. The polymerization of laccase-treated lignans was evidenced by size exclusion chromatography, reversed phase - high performance liquid chromatography, and matrix-assisted laser desorption/ionisation - time of flight mass spectrometry. The data showed that the selected substrates could be oxidised by laccase. Secoisolariciresinol and secoisolariciresinol diglucoside were polymerized by laccase to a similar extent. The lignan macromolecule reacted to a lesser extent. Polymerization of the macromolecule proceeded mainly via its secoisolariciresinol diglucoside moieties. Furthermore, it was shown that ferulic acid can be linked to polymerized secoisolariciresinol via decarboxylation by laccase. This investigation showed that lignans can be enzymatically modified by Trametes hirsuta laccase.

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KW - laccase

KW - polymerization

KW - SEC

KW - MALDI-TOF MS

KW - FTIR

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JO - BioResources

JF - BioResources

SN - 1930-2126

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Mattinen M-L, Struijs K, Suortti T, Mattila I, Kruus K, Willför S et al. Modification of lignans by Trametes hirsuta laccase. BioResources. 2009;4(2):482-496.