Thermostable laccases produbed by a white-rot fungus from Peniophora species

Marja-Leena Niku-Paavola (Corresponding Author), Richard Fagerström, Kristiina Kruus, Liisa Viikari

Research output: Contribution to journalArticleScientificpeer-review

23 Citations (Scopus)

Abstract

A strain of Peniophora species was shown to produce laccase, which is a new feature for this species. Peniophora secreted several laccase isoforms with pI-values 3.7–4.2 when grown on glucose and soya meal medium. The Peniophora laccases were typical for Basidiomycetes with respect to pH-dependence, specific activity and inhibitors. The interesting exceptional feature of Peniophora laccases was their good thermostability. At 60 °C, the half-life of the isoforms in the culture filtrate was approximately 5 h and at 70 °C for 15 min. Also, the isolated main isoform with pI-value 4.1 and molecular mass 63 kDa was similarly thermostable. The N-terminal amino acid sequence, altogether 22 amino acid residues, of the separated isoform was 50–63% identical with those of the Basidiomycete laccases analyzed recently.

Original languageEnglish
Pages (from-to)100 - 102
Number of pages3
JournalEnzyme and Microbial Technology
Volume35
Issue number1
DOIs
Publication statusPublished - 2004
MoE publication typeA1 Journal article-refereed

Fingerprint

Laccase
Fungi
Amino acids
Protein Isoforms
Molecular mass
Basidiomycota
Glucose
Amino Acids
Half-Life
Meals
Amino Acid Sequence

Keywords

  • Peniophora
  • Laccase
  • Thermostability

Cite this

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title = "Thermostable laccases produbed by a white-rot fungus from Peniophora species",
abstract = "A strain of Peniophora species was shown to produce laccase, which is a new feature for this species. Peniophora secreted several laccase isoforms with pI-values 3.7–4.2 when grown on glucose and soya meal medium. The Peniophora laccases were typical for Basidiomycetes with respect to pH-dependence, specific activity and inhibitors. The interesting exceptional feature of Peniophora laccases was their good thermostability. At 60 °C, the half-life of the isoforms in the culture filtrate was approximately 5 h and at 70 °C for 15 min. Also, the isolated main isoform with pI-value 4.1 and molecular mass 63 kDa was similarly thermostable. The N-terminal amino acid sequence, altogether 22 amino acid residues, of the separated isoform was 50–63{\%} identical with those of the Basidiomycete laccases analyzed recently.",
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Thermostable laccases produbed by a white-rot fungus from Peniophora species. / Niku-Paavola, Marja-Leena (Corresponding Author); Fagerström, Richard; Kruus, Kristiina; Viikari, Liisa.

In: Enzyme and Microbial Technology, Vol. 35, No. 1, 2004, p. 100 - 102.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Thermostable laccases produbed by a white-rot fungus from Peniophora species

AU - Niku-Paavola, Marja-Leena

AU - Fagerström, Richard

AU - Kruus, Kristiina

AU - Viikari, Liisa

PY - 2004

Y1 - 2004

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AB - A strain of Peniophora species was shown to produce laccase, which is a new feature for this species. Peniophora secreted several laccase isoforms with pI-values 3.7–4.2 when grown on glucose and soya meal medium. The Peniophora laccases were typical for Basidiomycetes with respect to pH-dependence, specific activity and inhibitors. The interesting exceptional feature of Peniophora laccases was their good thermostability. At 60 °C, the half-life of the isoforms in the culture filtrate was approximately 5 h and at 70 °C for 15 min. Also, the isolated main isoform with pI-value 4.1 and molecular mass 63 kDa was similarly thermostable. The N-terminal amino acid sequence, altogether 22 amino acid residues, of the separated isoform was 50–63% identical with those of the Basidiomycete laccases analyzed recently.

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KW - Laccase

KW - Thermostability

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