Production and characterization of cellobiose dehydrogenase from Phanerochaete chrysosporium KCCM 60256 and its application for an enzymatic fuel cell

Han Suk Choi, Dong Sup Kim, Laxmi Prasad Thapa, Sang Jun Lee, Sung Bong Kim, Jaehoon Cho, Chulhwan Park, Seung Wook Kim

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9 Citations (Scopus)


The enzyme cellobiose dehydrogenase (CDH), with high ability of electron transport, has been widely used in enzymatic fuel cells or biosensors. In this study, the cellobiose dehydrogenase gene from Phanerochaete chrysosporium KCCM 60256 was amplified and expressed in the methylotrophic yeast Pichia pastoris X-33. The recombinant enzyme (PcCDH) was purified using a metal affinity chromatography under non-denaturing conditions. The purified enzyme was analyzed by SDS-PAGE, confirming a corresponding band about 100 kDa. The enzyme activity of this purified PcCDH was determined as 1,845U/L (65mg/L protein). The enzyme showed the maximum activity at pH 4.5 and high activity in broad ranges of temperature from 30°C to 60°C. Moreover, the application of PcCDH to enzymatic fuel cell (EFC) was demonstrated. Lactose was used as the substrate in the EFC system; anode and cathode were immobilized with PcCDH and laccase, respectively. The cell’s open circuit voltage and maximum power density of the EFC system were, respectively, determined as 0.435 V and 314 μW/cm2 (at 0.247 V) with 10 mM lactose.

Original languageEnglish
Pages (from-to)1-8
Number of pages8
JournalKorean Journal of Chemical Engineering
Publication statusAccepted/In press - 2016 Sep 3



  • Cellobiose Dehydrogenase
  • Enzymatic Fuel Cell
  • Phanerochaete chrysosporium
  • Pichia pastoris

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

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