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      KCI등재 SCIE SCOPUS

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

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      https://www.riss.kr/link?id=A103562250

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      다국어 초록 (Multilingual Abstract)

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      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 oC to 60 oC. 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.
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      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 ...

      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 oC to 60 oC. 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.

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      참고문헌 (Reference)

      1 B. Mathieu, 10 : 113-, 2011

      2 G. D. Jones, 256 : 713-, 1988

      3 Desriani, 391 : 46-, 2010

      4 K. Igarashi, 274 : 3338-, 1999

      5 B. M. Hallberg, 8 : 79-, 2000

      6 G. Henriksson, 78 : 93-, 2000

      7 G. Henriksson, 1383 : 48-, 1998

      8 G. Henriksson, 42 : 790-, 1995

      9 A. Leonowicz, 27 : 175-, 1999

      10 F. Huang, 46 : 1956-, 2001

      1 B. Mathieu, 10 : 113-, 2011

      2 G. D. Jones, 256 : 713-, 1988

      3 Desriani, 391 : 46-, 2010

      4 K. Igarashi, 274 : 3338-, 1999

      5 B. M. Hallberg, 8 : 79-, 2000

      6 G. Henriksson, 78 : 93-, 2000

      7 G. Henriksson, 1383 : 48-, 1998

      8 G. Henriksson, 42 : 790-, 1995

      9 A. Leonowicz, 27 : 175-, 1999

      10 F. Huang, 46 : 1956-, 2001

      11 E. Kim, 17 : 55-, 2012

      12 J. Sulej, 176 : 1638-, 2015

      13 R. Ludwig, 405 : 3637-, 2013

      14 I. J. Szabo, 48 : 221-, 1996

      15 U. Baminger, 35 : 253-, 1999

      16 H. U. Lee, 42 : 342-, 2013

      17 D. S. Kim, 162 : G113-, 2015

      18 J. Y. Lee, 26 : 2658-, 2011

      19 J. L. Cereghino, 24 : 45-, 2000

      20 R. Gachhui, 271 : 594-, 1996

      21 A. Leber, 274 : 58-, 1999

      22 V. Coman, 10 : 6093-, 2008

      23 F. Tasca, 112 : 13668-, 2008

      24 F. Tasca, 81 : 2791-, 2009

      25 U. Salaj-Kosla, 405 : 3823-, 2013

      26 Z. Ruifu, 75 : 63-, 2011

      27 W. Harreither, 7 : 1359-, 2012

      28 N. Kannan, 6 : 979-, 2009

      29 A. Batra, 40 : 1533-, 2005

      30 M. Samejima, 207 : 103-, 1992

      31 Eun Ji Kim, "Enhanced production of cellobiose dehydrogenase and β-glucosidase by Phanerochaete chrysosporium" 한국화학공학회 29 (29): 77-81, 2012

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      공동연구자 (7)

      유사연구자 (20) 활용도상위20명

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      학술지 이력

      학술지 이력
      연월일 이력구분 이력상세 등재구분
      2023 평가예정 해외DB학술지평가 신청대상 (해외등재 학술지 평가)
      2020-01-01 평가 등재학술지 유지 (해외등재 학술지 평가) KCI등재
      2016-06-21 학술지명변경 한글명 : The Korean Journal of Chemical Engineering -> Korean Journal of Chemical Engineering
      외국어명 : The Korean Journal of Chemical Engineering -> Korean Journal of Chemical Engineering      		 KCI등재
      2011-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2009-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2007-09-27 학회명변경 영문명 : The Korean Institute Of Chemical Engineers -> The Korean Institute of Chemical Engineers KCI등재
      2007-09-03 학술지명변경 한글명 : The Korean Journal of Chemical Engineeri -> The Korean Journal of Chemical Engineering
      외국어명 : The Korean Journal of Chemical Engineeri -> The Korean Journal of Chemical Engineering      		 KCI등재
      2007-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2005-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2002-01-01 평가 등재학술지 선정 (등재후보2차) KCI등재
      1999-07-01 평가 등재후보학술지 선정 (신규평가) KCI등재후보
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      학술지 인용정보

      학술지 인용정보
      기준연도 WOS-KCI 통합IF(2년) KCIF(2년) KCIF(3년)
      2016 1.92 0.72 1.4
      KCIF(4년) KCIF(5년) 중심성지수(3년) 즉시성지수
      1.15 0.94 0.403 0.14
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