Journal Article
- Biotransformation of (-)-α-pinene and geraniol to α-terpineol and p-menthane-3,8-diol by the white rot fungus, Polyporus brumalis
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Su-Yeon Lee , Seon-Hong Kim , Chang-Young Hong , Se-Yeong Park , In-Gyu Choi
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J. Microbiol. 2015;53(7):462-467. Published online June 27, 2015
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DOI: https://doi.org/10.1007/s12275-015-5081-9
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Abstract
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In this study, the monoterpenes, α-pinene and geraniol, were
biotransformed to synthesize monoterpene alcohol compounds.
Polyporus brumalis which is classified as a white rot
fungus was used as a biocatalyst. Consequently α-terpineol
was synthesized from α-pinene by P. brumalis mycelium,
after three days. Moreover, another substrate, the acyclic
monoterpenoids geraniol was transformed into the cyclic
compound, p-menthane-3, 8-diol (PMD). The main metabolites,
i.e., α-terpineol and PMD, are known to be bioactive
monoterpene alcohol compounds. This study highlights the
potential of fungal biocatalysts for monoterpene transformation.
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Citations
Citations to this article as recorded by

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Research Support, Non-U.S. Gov't
- The First Report of Two Species of Polyporus (Polyporaceae, Basidiomycota) from South Korea
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Jin Sung Lee , Eun Ju Woo , Kyoung Hee Oh , Jae-Jin Kim , Young Woon Lim
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J. Microbiol. 2010;48(6):748-753. Published online January 9, 2011
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DOI: https://doi.org/10.1007/s12275-010-0105-y
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Abstract
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Based on morphological examination, two species of Polyporus, P. dictyopus, and P. tuberaster, were identified, which constitutes the first record of these species in South Korea. To confirm their affinity within the genus Polyporus, the phylogenetic relationships of Polyporus and allied genera were established from nuclear large
subunit ribosomal DNA (nLSU rDNA) sequences, and a morphological diagnostic key is presented to clarify the Korean species of Polyporus.
Journal Article
- Molecular Characteristics of Two Laccase from the Basidiomycete Fungus Polyporus brumalis
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Sun-Hwa Ryu , A-Young Lee , Myungkil Kim
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J. Microbiol. 2008;46(1):62-69.
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DOI: https://doi.org/10.1007/s12275-007-0110-y
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Abstract
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Two laccase cDNAs, pblac1 and pblac2, were cloned from a white-rot fungus strain, Polyporus brumalis (KFRI 20912). The cloned cDNAs consisted of 1,829 bp and 1,804 bp, and their open reading frames encoded proteins of 520 and 524 amino acids, with calculated molecular masses of approximately 55.9 kDa and 56 kDa, respectively. The deduced amino acid sequences of each protein showed 70% similarity. The copper binding regions were conserved in both proteins, as in other fungal laccases. RT-PCR analysis revealed that the transcript levels of the two laccases increased progressively in shallow stationary culture liquid medium. The transcript level of each laccase was induced when the fungus was exposed to di-butyl phthalate (DBP), suggesting that the two laccases are involved in DBP degradation. The overexpression of the pblac1 gene was derived by the promoter of a gene for glyceraldehyde-3-phosphate dehydrogenase, using a homologous system. The activity of laccase in the transformants was significantly higher than that of the wild type. The identification of these laccase cDNAs was a first step to characterize the molecular events related to the lignin degradation ability of this basidiomycetous fungus, as well as the degradation of many recalcitrant xenobiotics.