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Production and induction of manganese peroxidase isozymes in a white-rot fungus Pleurotus ostreatus

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Abstract

The production of MnP by Pleurotus ostreatus in different liquid cultures was investigated. The highest level of activity was observed after 8 days of culture in peptone-glucose-yeast extract medium (PGY), whereas maximal activity was achieved after 30 days in glucose-yeast extract medium (GY). MnP was purified to homogeneity from PGY (designated MnP-PGY) and GY (MnP-GY). The isoelectric points of MnP-PGY and MnP-GY were 3.77 and 4.06, respectively. The molecular mass of both enzymes was 42 kDa. Analysis of the N-terminal amino acid sequence of purified MnPs and nucleotide sequence of cloned mnp indicated that MnP-GY has VTCATGQTTANE at the N-terminus, whereas MnP-PGY has ATCADGRTTANA. A putative exposed tryptophan residue (W170) was found in MnP-GY. Both isozymes oxidized veratryl alcohol, although the K m of MnP-GY was lower than that of MnP-PGY. Thus, the presence of peptone in the medium affected the production of MnP isozymes. Reverse transcription-polymerase chain reaction (RT-PCR) analysis indicated that the synthesis of MnP isozymes is controlled by culture conditions at the transcriptional level.

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Authors and Affiliations

  1. Laboratory of Biomass Conversion, Kyoto University, Wood Research Institute, Gokasho Uji, Kyoto 611-0011, Japan

    H. Kamitsuji, Y. Honda & T. Watanabe

  2. Institute of Wood Technology, Akita Prefectural University, Noshiro, Akita 016-0876, Japan

    M. Kuwahara

Authors
  1. H. Kamitsuji
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  2. Y. Honda
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  3. T. Watanabe
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  4. M. Kuwahara
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Correspondence to M. Kuwahara.

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Kamitsuji, H., Honda, Y., Watanabe, T. et al. Production and induction of manganese peroxidase isozymes in a white-rot fungus Pleurotus ostreatus . Appl Microbiol Biotechnol 65, 287–294 (2004). https://doi.org/10.1007/s00253-003-1543-9

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  • DOI: https://doi.org/10.1007/s00253-003-1543-9

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