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2 "Polyporus brumalis"
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Biotransformation of (-)-α-pinene and geraniol to α-terpineol and p-menthane-3,8-diol by the white rot fungus, Polyporus brumalis
Su-Yeon Lee , Seon-Hong Kim , Chang-Young Hong , Se-Yeong Park , In-Gyu Choi
J. Microbiol. 2015;53(7):462-467.   Published online June 27, 2015
DOI: https://doi.org/10.1007/s12275-015-5081-9
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  • 16 Crossref
AbstractAbstract
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.

Citations

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  • Biotransformation of terpene and terpenoid derivatives by Aspergillus niger NRRL 326
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  • Optimization of limonene biotransformation for the production of bulk amounts of α-terpineol
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  • Transcriptomic analysis of the white rot fungus Polyporus brumalis provides insight into sesquiterpene biosynthesis
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Molecular Characteristics of Two Laccase from the Basidiomycete Fungus Polyporus brumalis
Sun-Hwa Ryu , A-Young Lee , Myungkil Kim
J. Microbiol. 2008;46(1):62-69.
DOI: https://doi.org/10.1007/s12275-007-0110-y
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  • 14 Scopus
AbstractAbstract
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.

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