A novel enzyme-immobilization method for a biofuel cell

Jin Young Lee, Hyun Yong Shin, Jong Ho Lee, Yoon Seok Song, Seong Woo Kang, Chulhwan Park, Jung Bae Kim, Seung Wook Kim

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)


Biofuel cells utilizing biocatalysts are attractive alternatives to metal catalyst-based cells because of environmentally friendly cells and their renewability and good operations at room temperatures, even though they provide a low level of electrical power. In this study, the effect of a novel enzyme immobilization method on anodic electrical properties was evaluated under ambient conditions for increasing the power of an enzyme-based biofuel cell. The anodic system employed in the cell contained a gold electrode, pyrroloquinoline quinone (PQQ) as the electron transfer mediator, lactate dehydrogenase (LDH), β-nicotinamide adenine dinucleotide (NAD+) as the cofactor, and lactate as the substrate. The anodic electrical properties increased as a result of the novel enzyme-immobilization method. Furthermore, lactate, NAD+, or CaCl2, which can all influence enzyme activation, were used to prevent covalent bond formation near the active site of the LDH during enzyme-immobilization. Protection of the active site of the LDH using this novel enzyme-immobilization method increased its stability, which enabled to increase power production (142 μW/cm2) in a basic enzymatic fuel cell (EFC).

Original languageEnglish
Pages (from-to)274-278
Number of pages5
JournalJournal of Molecular Catalysis B: Enzymatic
Issue number4
Publication statusPublished - 2009 Aug


  • Enzyme stability
  • Immobilization
  • Lactate dehydrogenase
  • Pyrroloquinoline quinone
  • β-Nicotinamide adenine dinucleotide

ASJC Scopus subject areas

  • Catalysis
  • Bioengineering
  • Biochemistry
  • Process Chemistry and Technology


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