Heterologous expression of two ferulic acid esterases from Penicillium funiculosum

Applied Biochemistry and Biotechnology
Eric P KnoshaugWilliam S Adney

Abstract

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.

References

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Citations

Aug 12, 2010·Bioscience, Biotechnology, and Biochemistry·Kohsuke HashimotoMakoto Yoshida
Feb 4, 2010·Applied Microbiology and Biotechnology·Kofi AbokitsePeter C K Lau
Jun 30, 2009·Protein Expression and Purification·Fabio M SquinaRolf A Prade
Jun 26, 2015·Bioscience, Biotechnology, and Biochemistry·Masahiro WatanabeKazuhiko Ishikawa
Nov 28, 2014·Microbiology and Molecular Biology Reviews : MMBR·Fernando SegatoRolf A Prade
Sep 20, 2011·Applied Biochemistry and Biotechnology·Meiqun WuPeter C K Lau

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