Heterologous expression of two ferulic acid esterases from Penicillium funiculosum

Appl Biochem Biotechnol. 2008 Mar;146(1-3):79-87. doi: 10.1007/s12010-007-8074-2. Epub 2007 Dec 7.


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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adsorption
  • Aspergillus / genetics*
  • Aspergillus / metabolism*
  • Binding Sites
  • Carboxylic Ester Hydrolases / chemistry*
  • Carboxylic Ester Hydrolases / genetics
  • Carboxylic Ester Hydrolases / metabolism*
  • Cellulose / chemistry*
  • Enzyme Activation
  • Enzyme Stability
  • Enzymes, Immobilized / chemistry
  • Penicillium / classification
  • Penicillium / genetics*
  • Penicillium / metabolism*
  • Protein Binding
  • Protein Engineering / methods
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Species Specificity
  • Substrate Specificity


  • Enzymes, Immobilized
  • Recombinant Proteins
  • Cellulose
  • Carboxylic Ester Hydrolases
  • feruloyl esterase