Manganese peroxidase of Agaricus bisporus: Grain bran-promoted production and gene characterization

Pauliina Lankinen (Corresponding Author), Kristiina Hildén, Nina Aro, Mirja Salkinoja-Salonen, Annele Hatakka

Research output: Contribution to journalArticleScientificpeer-review

29 Citations (Scopus)

Abstract

The main manganese peroxidase (MnP) isoenzyme of Agaricus bisporus ATCC 62459 produced in lignocellulose-containing cultures was isolated, cloned and sequenced. In liquid medium, where MnP was previously detected only in trace amounts, the production of MnP was enhanced by rye and wheat bran supplements. The pI (3.25) and N-terminal amino acid sequence (25 aa) of the enzyme from bran-containing cultures were identical to those reported from compost-isolated MnP1. MnP1 is a 328-aa long polypeptide preceded by a 26-aa leader peptide. The nucleotide sequence and putative amino acid sequence of MnP1 reveal its similarity to Pleurotus ostreatus MnP3 (62.5%), Lepista irina versatile peroxidase (VP) (61.8%) and Pleurotus eryngii VPs VPL2 and VPL1 (61.9% and 61.2%, respectively). The intron-exon structure resembles that of P. ostreatus MnP1 and P. eryngii VPL1. Despite the sequence similarity to VPs, in the A. bisporus MnP1 sequence, alanine (A163) is present instead of tryptophane (W164), distinguishing it from the veratryl alcohol oxidising P. eryngii VPLs. The MnP sequence can be used as a tool to examine the pattern of ligninolytic gene expression during the growth and fruiting of A. bisporus to optimise compost composition, fungal growth and mushroom production.
Original languageEnglish
Pages (from-to)401 - 407
Number of pages7
JournalApplied Microbiology and Biotechnology
Volume66
Issue number4
DOIs
Publication statusPublished - 2005
MoE publication typeA1 Journal article-refereed

Fingerprint

manganese peroxidase
Agaricus
Pleurotus
Genes
Amino Acid Sequence
Soil
Agaricales
Dietary Fiber
Growth
Protein Sorting Signals
Alanine
Introns
Peroxidase
Isoenzymes
Exons
Gene Expression
Peptides
Enzymes

Keywords

  • manganese oxidizing bacteria
  • peroxidase
  • Agaricus bisporus

Cite this

Lankinen, Pauliina ; Hildén, Kristiina ; Aro, Nina ; Salkinoja-Salonen, Mirja ; Hatakka, Annele. / Manganese peroxidase of Agaricus bisporus : Grain bran-promoted production and gene characterization. In: Applied Microbiology and Biotechnology. 2005 ; Vol. 66, No. 4. pp. 401 - 407.
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abstract = "The main manganese peroxidase (MnP) isoenzyme of Agaricus bisporus ATCC 62459 produced in lignocellulose-containing cultures was isolated, cloned and sequenced. In liquid medium, where MnP was previously detected only in trace amounts, the production of MnP was enhanced by rye and wheat bran supplements. The pI (3.25) and N-terminal amino acid sequence (25 aa) of the enzyme from bran-containing cultures were identical to those reported from compost-isolated MnP1. MnP1 is a 328-aa long polypeptide preceded by a 26-aa leader peptide. The nucleotide sequence and putative amino acid sequence of MnP1 reveal its similarity to Pleurotus ostreatus MnP3 (62.5{\%}), Lepista irina versatile peroxidase (VP) (61.8{\%}) and Pleurotus eryngii VPs VPL2 and VPL1 (61.9{\%} and 61.2{\%}, respectively). The intron-exon structure resembles that of P. ostreatus MnP1 and P. eryngii VPL1. Despite the sequence similarity to VPs, in the A. bisporus MnP1 sequence, alanine (A163) is present instead of tryptophane (W164), distinguishing it from the veratryl alcohol oxidising P. eryngii VPLs. The MnP sequence can be used as a tool to examine the pattern of ligninolytic gene expression during the growth and fruiting of A. bisporus to optimise compost composition, fungal growth and mushroom production.",
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author = "Pauliina Lankinen and Kristiina Hild{\'e}n and Nina Aro and Mirja Salkinoja-Salonen and Annele Hatakka",
year = "2005",
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language = "English",
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Manganese peroxidase of Agaricus bisporus : Grain bran-promoted production and gene characterization. / Lankinen, Pauliina (Corresponding Author); Hildén, Kristiina; Aro, Nina; Salkinoja-Salonen, Mirja; Hatakka, Annele.

In: Applied Microbiology and Biotechnology, Vol. 66, No. 4, 2005, p. 401 - 407.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Manganese peroxidase of Agaricus bisporus

T2 - Grain bran-promoted production and gene characterization

AU - Lankinen, Pauliina

AU - Hildén, Kristiina

AU - Aro, Nina

AU - Salkinoja-Salonen, Mirja

AU - Hatakka, Annele

PY - 2005

Y1 - 2005

N2 - The main manganese peroxidase (MnP) isoenzyme of Agaricus bisporus ATCC 62459 produced in lignocellulose-containing cultures was isolated, cloned and sequenced. In liquid medium, where MnP was previously detected only in trace amounts, the production of MnP was enhanced by rye and wheat bran supplements. The pI (3.25) and N-terminal amino acid sequence (25 aa) of the enzyme from bran-containing cultures were identical to those reported from compost-isolated MnP1. MnP1 is a 328-aa long polypeptide preceded by a 26-aa leader peptide. The nucleotide sequence and putative amino acid sequence of MnP1 reveal its similarity to Pleurotus ostreatus MnP3 (62.5%), Lepista irina versatile peroxidase (VP) (61.8%) and Pleurotus eryngii VPs VPL2 and VPL1 (61.9% and 61.2%, respectively). The intron-exon structure resembles that of P. ostreatus MnP1 and P. eryngii VPL1. Despite the sequence similarity to VPs, in the A. bisporus MnP1 sequence, alanine (A163) is present instead of tryptophane (W164), distinguishing it from the veratryl alcohol oxidising P. eryngii VPLs. The MnP sequence can be used as a tool to examine the pattern of ligninolytic gene expression during the growth and fruiting of A. bisporus to optimise compost composition, fungal growth and mushroom production.

AB - The main manganese peroxidase (MnP) isoenzyme of Agaricus bisporus ATCC 62459 produced in lignocellulose-containing cultures was isolated, cloned and sequenced. In liquid medium, where MnP was previously detected only in trace amounts, the production of MnP was enhanced by rye and wheat bran supplements. The pI (3.25) and N-terminal amino acid sequence (25 aa) of the enzyme from bran-containing cultures were identical to those reported from compost-isolated MnP1. MnP1 is a 328-aa long polypeptide preceded by a 26-aa leader peptide. The nucleotide sequence and putative amino acid sequence of MnP1 reveal its similarity to Pleurotus ostreatus MnP3 (62.5%), Lepista irina versatile peroxidase (VP) (61.8%) and Pleurotus eryngii VPs VPL2 and VPL1 (61.9% and 61.2%, respectively). The intron-exon structure resembles that of P. ostreatus MnP1 and P. eryngii VPL1. Despite the sequence similarity to VPs, in the A. bisporus MnP1 sequence, alanine (A163) is present instead of tryptophane (W164), distinguishing it from the veratryl alcohol oxidising P. eryngii VPLs. The MnP sequence can be used as a tool to examine the pattern of ligninolytic gene expression during the growth and fruiting of A. bisporus to optimise compost composition, fungal growth and mushroom production.

KW - manganese oxidizing bacteria

KW - peroxidase

KW - Agaricus bisporus

U2 - 10.1007/s00253-004-1731-2

DO - 10.1007/s00253-004-1731-2

M3 - Article

VL - 66

SP - 401

EP - 407

JO - Applied Microbiology and Biotechnology

JF - Applied Microbiology and Biotechnology

SN - 0175-7598

IS - 4

ER -