A novel laccase from the ascomycete Melanocarpus albomyces

Kristiina Kruus, Laura-Leena Kiiskinen, Markku Saloheimo, Nina Hakulinen, Juha Rouvinen, Arja Paananen, Markus Linder, Liisa Viikari

Research output: Chapter in Book/Report/Conference proceedingConference article in proceedingsScientificpeer-review

Abstract

A novel laccase from the ascomycete Melanocarpus albomyces was isolated, purified and characterized. The ultraviolet-visible absorption and electron paramagnetic resonance spectra indicated that the three types of coppers were present. Redox potential of the T1 copper of M. albomyces laccase was determined to be 0.46±0.01 V. The enzyme had very interesting pH and temperature behaviour. It had a pH optimum measured with guaiacol at neutral and slightly alkalic pH and substantial activity still at pH 8. The laccase showed very good thermostability, retaining full activity for two hours at 60°C. The gene encoding the M. albomyces laccase was isolated and sequenced. The length of the open reading frame of the M. albomyces laccase was 623 amino acid residues. The copper binding residues were well conserved and the amino acid sequence had high homology to other ascomycete laccases. Interestingly the secreted laccase was processed both from the amino and carboxy terminus. The laccase was also crystallized with all four coppers present.
Original languageEnglish
Title of host publicationApplications of Enzymes to Lignocellulosics
EditorsShawn D. Mansfield, John N. Saddler
Place of PublicationWashington, DC
PublisherAmerican Chemical Society ACS
Chapter19
Pages315-331
ISBN (Electronic)978-0-8412-1960-1
ISBN (Print)978-0-8412-3831-2
DOIs
Publication statusPublished - 2003
MoE publication typeA4 Article in a conference publication

Publication series

SeriesACS Symposium Series
Volume855

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laccase
Ascomycota
copper
guaiacol
electron paramagnetic resonance spectroscopy
redox potential
thermal stability
open reading frames
amino acid sequences
amino acids
enzymes

Cite this

Kruus, K., Kiiskinen, L-L., Saloheimo, M., Hakulinen, N., Rouvinen, J., Paananen, A., ... Viikari, L. (2003). A novel laccase from the ascomycete Melanocarpus albomyces. In S. D. Mansfield, & J. N. Saddler (Eds.), Applications of Enzymes to Lignocellulosics (pp. 315-331). Washington, DC: American Chemical Society ACS. ACS Symposium Series, Vol.. 855 https://doi.org/10.1021/bk-2003-0855.ch019
Kruus, Kristiina ; Kiiskinen, Laura-Leena ; Saloheimo, Markku ; Hakulinen, Nina ; Rouvinen, Juha ; Paananen, Arja ; Linder, Markus ; Viikari, Liisa. / A novel laccase from the ascomycete Melanocarpus albomyces. Applications of Enzymes to Lignocellulosics. editor / Shawn D. Mansfield ; John N. Saddler. Washington, DC : American Chemical Society ACS, 2003. pp. 315-331 (ACS Symposium Series, Vol. 855).
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title = "A novel laccase from the ascomycete Melanocarpus albomyces",
abstract = "A novel laccase from the ascomycete Melanocarpus albomyces was isolated, purified and characterized. The ultraviolet-visible absorption and electron paramagnetic resonance spectra indicated that the three types of coppers were present. Redox potential of the T1 copper of M. albomyces laccase was determined to be 0.46±0.01 V. The enzyme had very interesting pH and temperature behaviour. It had a pH optimum measured with guaiacol at neutral and slightly alkalic pH and substantial activity still at pH 8. The laccase showed very good thermostability, retaining full activity for two hours at 60°C. The gene encoding the M. albomyces laccase was isolated and sequenced. The length of the open reading frame of the M. albomyces laccase was 623 amino acid residues. The copper binding residues were well conserved and the amino acid sequence had high homology to other ascomycete laccases. Interestingly the secreted laccase was processed both from the amino and carboxy terminus. The laccase was also crystallized with all four coppers present.",
author = "Kristiina Kruus and Laura-Leena Kiiskinen and Markku Saloheimo and Nina Hakulinen and Juha Rouvinen and Arja Paananen and Markus Linder and Liisa Viikari",
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Kruus, K, Kiiskinen, L-L, Saloheimo, M, Hakulinen, N, Rouvinen, J, Paananen, A, Linder, M & Viikari, L 2003, A novel laccase from the ascomycete Melanocarpus albomyces. in SD Mansfield & JN Saddler (eds), Applications of Enzymes to Lignocellulosics. American Chemical Society ACS, Washington, DC, ACS Symposium Series, vol. 855, pp. 315-331. https://doi.org/10.1021/bk-2003-0855.ch019

A novel laccase from the ascomycete Melanocarpus albomyces. / Kruus, Kristiina; Kiiskinen, Laura-Leena; Saloheimo, Markku; Hakulinen, Nina; Rouvinen, Juha; Paananen, Arja; Linder, Markus; Viikari, Liisa.

Applications of Enzymes to Lignocellulosics. ed. / Shawn D. Mansfield; John N. Saddler. Washington, DC : American Chemical Society ACS, 2003. p. 315-331 (ACS Symposium Series, Vol. 855).

Research output: Chapter in Book/Report/Conference proceedingConference article in proceedingsScientificpeer-review

TY - GEN

T1 - A novel laccase from the ascomycete Melanocarpus albomyces

AU - Kruus, Kristiina

AU - Kiiskinen, Laura-Leena

AU - Saloheimo, Markku

AU - Hakulinen, Nina

AU - Rouvinen, Juha

AU - Paananen, Arja

AU - Linder, Markus

AU - Viikari, Liisa

PY - 2003

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N2 - A novel laccase from the ascomycete Melanocarpus albomyces was isolated, purified and characterized. The ultraviolet-visible absorption and electron paramagnetic resonance spectra indicated that the three types of coppers were present. Redox potential of the T1 copper of M. albomyces laccase was determined to be 0.46±0.01 V. The enzyme had very interesting pH and temperature behaviour. It had a pH optimum measured with guaiacol at neutral and slightly alkalic pH and substantial activity still at pH 8. The laccase showed very good thermostability, retaining full activity for two hours at 60°C. The gene encoding the M. albomyces laccase was isolated and sequenced. The length of the open reading frame of the M. albomyces laccase was 623 amino acid residues. The copper binding residues were well conserved and the amino acid sequence had high homology to other ascomycete laccases. Interestingly the secreted laccase was processed both from the amino and carboxy terminus. The laccase was also crystallized with all four coppers present.

AB - A novel laccase from the ascomycete Melanocarpus albomyces was isolated, purified and characterized. The ultraviolet-visible absorption and electron paramagnetic resonance spectra indicated that the three types of coppers were present. Redox potential of the T1 copper of M. albomyces laccase was determined to be 0.46±0.01 V. The enzyme had very interesting pH and temperature behaviour. It had a pH optimum measured with guaiacol at neutral and slightly alkalic pH and substantial activity still at pH 8. The laccase showed very good thermostability, retaining full activity for two hours at 60°C. The gene encoding the M. albomyces laccase was isolated and sequenced. The length of the open reading frame of the M. albomyces laccase was 623 amino acid residues. The copper binding residues were well conserved and the amino acid sequence had high homology to other ascomycete laccases. Interestingly the secreted laccase was processed both from the amino and carboxy terminus. The laccase was also crystallized with all four coppers present.

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M3 - Conference article in proceedings

SN - 978-0-8412-3831-2

T3 - ACS Symposium Series

SP - 315

EP - 331

BT - Applications of Enzymes to Lignocellulosics

A2 - Mansfield, Shawn D.

A2 - Saddler, John N.

PB - American Chemical Society ACS

CY - Washington, DC

ER -

Kruus K, Kiiskinen L-L, Saloheimo M, Hakulinen N, Rouvinen J, Paananen A et al. A novel laccase from the ascomycete Melanocarpus albomyces. In Mansfield SD, Saddler JN, editors, Applications of Enzymes to Lignocellulosics. Washington, DC: American Chemical Society ACS. 2003. p. 315-331. (ACS Symposium Series, Vol. 855). https://doi.org/10.1021/bk-2003-0855.ch019