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Heterologous expression of a new manganese-dependent peroxidase gene from Peniophora incarnata KUC8836 and its ability to remove anthracene in Saccharomyces cerevisiae.
Lee, Aslan Hwanhwi; Kang, Chang-Min; Lee, Young Min; Lee, Hanbyul; Yun, Cheol-Won; Kim, Gyu-Hyeok; Kim, Jae-Jin.
Afiliación
  • Lee AH; Division of Environmental Science & Ecological Engineering, Korea University, 145 Anam-ro, Seongbuk-gu, Seoul 02841, South Korea.
  • Kang CM; School of Life Sciences and Biotechnology, Korea University, 145 Anam-ro, Seongbuk-gu, Seoul 02841, South Korea.
  • Lee YM; Division of Environmental Science & Ecological Engineering, Korea University, 145 Anam-ro, Seongbuk-gu, Seoul 02841, South Korea.
  • Lee H; Division of Environmental Science & Ecological Engineering, Korea University, 145 Anam-ro, Seongbuk-gu, Seoul 02841, South Korea.
  • Yun CW; School of Life Sciences and Biotechnology, Korea University, 145 Anam-ro, Seongbuk-gu, Seoul 02841, South Korea.
  • Kim GH; Division of Environmental Science & Ecological Engineering, Korea University, 145 Anam-ro, Seongbuk-gu, Seoul 02841, South Korea.
  • Kim JJ; Division of Environmental Science & Ecological Engineering, Korea University, 145 Anam-ro, Seongbuk-gu, Seoul 02841, South Korea. Electronic address: jae-jinkim@korea.ac.kr.
J Biosci Bioeng ; 122(6): 716-721, 2016 Dec.
Article en En | MEDLINE | ID: mdl-27353859
The white rot fungus Peniophora incarnata KUC8836 has received an attention as the greatest degrader of polycyclic aromatic hydrocarbons (PAHs), which are hazardous xenobiotics and recalcitrant pollutants. To characterize the mechanisms through which MnP degrades PAHs, heterologous expression of manganese-dependent peroxidase (MnP) gene pimp1 was performed in Saccharomyces cerevisiae BY4741 via the pGEM-T Easy vector, resulting in the recombinant plasmid pESC-URA/pimp1 containing the MnP signal peptide. MnP was significantly secreted into the culture medium with galactose as an active protein with higher efficiency (3.58 U mL-1) by transformants than by the wild-type S. cerevisiae. The recombinant MnP protein was shown to have a molecular weight of 44 kDa by western blotting analysis. With regard to enhancing the bioremediation of PAHs in the environment, anthracene was effectively degraded by the MnP encoded by pimp1, with a degradation rate of 6.5% when Tween 80 was added. In addition, the MnP activity of the transformant exhibited the highest efficiency (2.49 U mL-1) during the degradation. These results show that pimp1 might be useful for biodegradation and gene expression technologies at a transcriptional level, and genetic approaches can be improved by incorporating the highly ligninolytic gene pimp1 and the fungus P. incarnata KUC8836.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Peroxidasas / Saccharomyces cerevisiae / Basidiomycota / Antracenos Idioma: En Revista: J Biosci Bioeng Asunto de la revista: ENGENHARIA BIOMEDICA / MICROBIOLOGIA Año: 2016 Tipo del documento: Article País de afiliación: Corea del Sur Pais de publicación: Japón

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Peroxidasas / Saccharomyces cerevisiae / Basidiomycota / Antracenos Idioma: En Revista: J Biosci Bioeng Asunto de la revista: ENGENHARIA BIOMEDICA / MICROBIOLOGIA Año: 2016 Tipo del documento: Article País de afiliación: Corea del Sur Pais de publicación: Japón