Action of fungal laccases on lignin model compounds in organic solvents

Pekka Maijala (Corresponding Author), Maija-Liisa Mattinen, Paula Nousiainen, Jussi Kontro, Janne Asikkala, Jussi Sipilä, Liisa Viikari

Research output: Contribution to journalArticleScientificpeer-review

18 Citations (Scopus)

Abstract

The stability and reactivity of five different thermostable fungal laccases from the species Trametes hirsuta, Melanocarpus albomyces, Thielavia arenaria (two laccases) and Chaetomium thermophilum were investigated in the presence of organic solvents. Oxidations of small organic phenolic compounds, matairesinol and 7-hydroxymatairesinol lignans, as well as synthetic lignin dehydrogenation polymer DHP in aqueous solutions of ethanol and propylene glycol solvents were investigated using analysis of oxidation rates, high performance liquid chromatography and size-exclusion chromatography. The laccases showed variability in their solvent tolerance. The redox potential of the laccases appeared not to be the main factor determining the efficiency of the polymerization reactions of complex phenolic model compounds in aqueous organic solutions. Nuclear magnetic resonance spectroscopic analysis of laccase treated DHP in 50% propylene glycol indicated that the formation of new biphenylic 5–5′ structures was favored in laccase-catalyzed radical coupling reactions over the other possible reactions through the phenolic groups forming new 5—O—4 ether bonds. The polymerization reactions took place even at high concentrations of solvents, which already inhibited the enzyme activity, encouraging enzymatic upgrading of lignin in organic solvents to be studied further. Thus, it was confirmed that thermostable laccases are potential enzymes for various industrial applications where organic solvents are required for the reaction systems.
Original languageEnglish
Pages (from-to)59-67
JournalJournal of Molecular Catalysis B: Enzymatic
Volume76
Issue number2
DOIs
Publication statusPublished - 2012
MoE publication typeA1 Journal article-refereed

Fingerprint

Laccase
Lignin
Organic solvents
Glycols
Propylene
Polymerization
Oxidation
Spectroscopic analysis
Size exclusion chromatography
High performance liquid chromatography
Enzyme activity
Propylene Glycol
Dehydrogenation
Industrial applications
Ethers
Ethanol
Enzymes
Nuclear magnetic resonance
Chaetomium
Trametes

Keywords

  • laccase
  • solvent
  • stability
  • reactivity
  • lignin
  • lignan

Cite this

Maijala, P., Mattinen, M-L., Nousiainen, P., Kontro, J., Asikkala, J., Sipilä, J., & Viikari, L. (2012). Action of fungal laccases on lignin model compounds in organic solvents. Journal of Molecular Catalysis B: Enzymatic, 76(2), 59-67. https://doi.org/10.1016/j.molcatb.2011.12.009
Maijala, Pekka ; Mattinen, Maija-Liisa ; Nousiainen, Paula ; Kontro, Jussi ; Asikkala, Janne ; Sipilä, Jussi ; Viikari, Liisa. / Action of fungal laccases on lignin model compounds in organic solvents. In: Journal of Molecular Catalysis B: Enzymatic. 2012 ; Vol. 76, No. 2. pp. 59-67.
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abstract = "The stability and reactivity of five different thermostable fungal laccases from the species Trametes hirsuta, Melanocarpus albomyces, Thielavia arenaria (two laccases) and Chaetomium thermophilum were investigated in the presence of organic solvents. Oxidations of small organic phenolic compounds, matairesinol and 7-hydroxymatairesinol lignans, as well as synthetic lignin dehydrogenation polymer DHP in aqueous solutions of ethanol and propylene glycol solvents were investigated using analysis of oxidation rates, high performance liquid chromatography and size-exclusion chromatography. The laccases showed variability in their solvent tolerance. The redox potential of the laccases appeared not to be the main factor determining the efficiency of the polymerization reactions of complex phenolic model compounds in aqueous organic solutions. Nuclear magnetic resonance spectroscopic analysis of laccase treated DHP in 50{\%} propylene glycol indicated that the formation of new biphenylic 5–5′ structures was favored in laccase-catalyzed radical coupling reactions over the other possible reactions through the phenolic groups forming new 5—O—4 ether bonds. The polymerization reactions took place even at high concentrations of solvents, which already inhibited the enzyme activity, encouraging enzymatic upgrading of lignin in organic solvents to be studied further. Thus, it was confirmed that thermostable laccases are potential enzymes for various industrial applications where organic solvents are required for the reaction systems.",
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Maijala, P, Mattinen, M-L, Nousiainen, P, Kontro, J, Asikkala, J, Sipilä, J & Viikari, L 2012, 'Action of fungal laccases on lignin model compounds in organic solvents', Journal of Molecular Catalysis B: Enzymatic, vol. 76, no. 2, pp. 59-67. https://doi.org/10.1016/j.molcatb.2011.12.009

Action of fungal laccases on lignin model compounds in organic solvents. / Maijala, Pekka (Corresponding Author); Mattinen, Maija-Liisa; Nousiainen, Paula; Kontro, Jussi; Asikkala, Janne; Sipilä, Jussi; Viikari, Liisa.

In: Journal of Molecular Catalysis B: Enzymatic, Vol. 76, No. 2, 2012, p. 59-67.

Research output: Contribution to journalArticleScientificpeer-review

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T1 - Action of fungal laccases on lignin model compounds in organic solvents

AU - Maijala, Pekka

AU - Mattinen, Maija-Liisa

AU - Nousiainen, Paula

AU - Kontro, Jussi

AU - Asikkala, Janne

AU - Sipilä, Jussi

AU - Viikari, Liisa

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N2 - The stability and reactivity of five different thermostable fungal laccases from the species Trametes hirsuta, Melanocarpus albomyces, Thielavia arenaria (two laccases) and Chaetomium thermophilum were investigated in the presence of organic solvents. Oxidations of small organic phenolic compounds, matairesinol and 7-hydroxymatairesinol lignans, as well as synthetic lignin dehydrogenation polymer DHP in aqueous solutions of ethanol and propylene glycol solvents were investigated using analysis of oxidation rates, high performance liquid chromatography and size-exclusion chromatography. The laccases showed variability in their solvent tolerance. The redox potential of the laccases appeared not to be the main factor determining the efficiency of the polymerization reactions of complex phenolic model compounds in aqueous organic solutions. Nuclear magnetic resonance spectroscopic analysis of laccase treated DHP in 50% propylene glycol indicated that the formation of new biphenylic 5–5′ structures was favored in laccase-catalyzed radical coupling reactions over the other possible reactions through the phenolic groups forming new 5—O—4 ether bonds. The polymerization reactions took place even at high concentrations of solvents, which already inhibited the enzyme activity, encouraging enzymatic upgrading of lignin in organic solvents to be studied further. Thus, it was confirmed that thermostable laccases are potential enzymes for various industrial applications where organic solvents are required for the reaction systems.

AB - The stability and reactivity of five different thermostable fungal laccases from the species Trametes hirsuta, Melanocarpus albomyces, Thielavia arenaria (two laccases) and Chaetomium thermophilum were investigated in the presence of organic solvents. Oxidations of small organic phenolic compounds, matairesinol and 7-hydroxymatairesinol lignans, as well as synthetic lignin dehydrogenation polymer DHP in aqueous solutions of ethanol and propylene glycol solvents were investigated using analysis of oxidation rates, high performance liquid chromatography and size-exclusion chromatography. The laccases showed variability in their solvent tolerance. The redox potential of the laccases appeared not to be the main factor determining the efficiency of the polymerization reactions of complex phenolic model compounds in aqueous organic solutions. Nuclear magnetic resonance spectroscopic analysis of laccase treated DHP in 50% propylene glycol indicated that the formation of new biphenylic 5–5′ structures was favored in laccase-catalyzed radical coupling reactions over the other possible reactions through the phenolic groups forming new 5—O—4 ether bonds. The polymerization reactions took place even at high concentrations of solvents, which already inhibited the enzyme activity, encouraging enzymatic upgrading of lignin in organic solvents to be studied further. Thus, it was confirmed that thermostable laccases are potential enzymes for various industrial applications where organic solvents are required for the reaction systems.

KW - laccase

KW - solvent

KW - stability

KW - reactivity

KW - lignin

KW - lignan

U2 - 10.1016/j.molcatb.2011.12.009

DO - 10.1016/j.molcatb.2011.12.009

M3 - Article

VL - 76

SP - 59

EP - 67

JO - Journal of Molecular Catalysis B: Enzymatic

JF - Journal of Molecular Catalysis B: Enzymatic

SN - 1381-1177

IS - 2

ER -