Heterologous Expression of Two Ferulic Acid Esterases from Penicillium Funiculosum

Eric P. Knoshaug, Michael J. Selig, John O. Baker, Stephen R. Decker, Michael E. Himmel, William S. Adney

Research output: Contribution to journalArticlepeer-review

17 Scopus Citations


Two recombinant ferulic acid esterases from Penicillium funiculosum produced in Aspergillus awamori were evaluated for their ability to improve the digestibility of pretreated corn stover. The genes, faeA and faeB, were cloned from P. funiculosum and expressed in A. awamori using their native signal sequences. Both enzymes contain a catalytic domain connected to a family 1 carbohydrate-binding module by a threonine-rich linker peptide. Interestingly, the carbohydrate binding-module is N-terminal in FaeA and C-terminal in FaeB. The enzymes were purified to homogeneity using column chromatography, and their thermal stability was characterized by differential scanning microcalorimetry. We evaluated both enzymes for their potential to enhance the cellulolytic activity of purified Trichoderma reesei Cel7A on pretreated corn stover.

Original languageAmerican English
Pages (from-to)79-87
Number of pages9
JournalApplied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology
Issue number1-3
StatePublished - 2008

NREL Publication Number

  • NREL/JA-510-43379


  • Biomass digestion
  • Cellulose
  • Ferulic acid esterase
  • Hemicellulose
  • Heterologous expression


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