Feruloyl esterase from Aspergillus clavatus improves xylan hydrolysis of sugarcane bagasse

Dyoni M. de Oliveira; Victor Hugo Salvador; Thatiane R. Mota; Aline Finger-Teixeira; Rodrigo F. de Almeida; Douglas A. A. Paixão; Amanda P. De Souza; Marcos S. Buckeridge; Rogério Marchiosi; Osvaldo Ferrarese-Filho; Fabio M. Squina; Wanderley D. dos Santos; Dyoni M. de Oliveira; Victor Hugo Salvador; Thatiane R. Mota; Aline Finger-Teixeira; Rodrigo F. de Almeida; Douglas A. A. Paixão; Amanda P. De Souza; Marcos S. Buckeridge; Rogério Marchiosi; Osvaldo Ferrarese-Filho; Fabio M. Squina; Wanderley D. dos Santos

doi:10.3934/bioeng.2017.1.1

AIMS Bioengineering

2017, Volume 4, Issue 1: 1-11. doi: 10.3934/bioeng.2017.1.1

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Research article

Feruloyl esterase from Aspergillus clavatus improves xylan hydrolysis of sugarcane bagasse

1.
Laboratory of Plant Biochemistry, State University of Maringá, Maringá, PR, Brazil
2.
Federal Institute of Education, Science and Technology, Paranavaí, PR, Brazil
3.
Brazilian Bioethanol Science and Technology Laboratory, Campinas, SP, Brazil
4.
Laboratory of Plant Physiological Ecology, University of São Paulo, São Paulo, SP, Brazil

Received: 25 September 2016 Accepted: 14 December 2016 Published: 22 December 2016

Feruloyl esterase is a subclass of carboxylic acid esterases with the capacity to release ferulic acid and other cinnamic acids from plant cell walls and synthetic substrates. Feruloyl esterases act synergistically with xylanases removing ferulic acid residues esterified to arabinoxylans. Feruloyl esterase type D from Aspergillus clavatus (AcFAE) was expressed in Escherichia coli, purified, and applied with a commercial xylanase consortium (Novozymes) for hydrolysis of sugarcane bagasse. Feruloyl esterase plus xylanase increased 5.13-fold the releasing of ferulic acid from sugarcane bagasse. Removal of only 7.7% of ferulic acid content by AcFAE increased 97.3% the sugarcane bagasse hydrolysis by xylanase. These data support the use of AcFAE as an interesting adjuvant enzyme to improve lignocellulose digestion and biotechnological tool for biorefineries.
- ferulic acid,
- feruloylated oligosaccharides,
- sugarcane biomass,
- lignocellulose,
- enzymatic hydrolysis
Citation: Dyoni M. de Oliveira, Victor Hugo Salvador, Thatiane R. Mota, Aline Finger-Teixeira, Rodrigo F. de Almeida, Douglas A. A. Paixão, Amanda P. De Souza, Marcos S. Buckeridge, Rogério Marchiosi, Osvaldo Ferrarese-Filho, Fabio M. Squina, Wanderley D. dos Santos. Feruloyl esterase from Aspergillus clavatus improves xylan hydrolysis of sugarcane bagasse[J]. AIMS Bioengineering, 2017, 4(1): 1-11. doi: 10.3934/bioeng.2017.1.1

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Abstract

Feruloyl esterase is a subclass of carboxylic acid esterases with the capacity to release ferulic acid and other cinnamic acids from plant cell walls and synthetic substrates. Feruloyl esterases act synergistically with xylanases removing ferulic acid residues esterified to arabinoxylans. Feruloyl esterase type D from Aspergillus clavatus (AcFAE) was expressed in Escherichia coli, purified, and applied with a commercial xylanase consortium (Novozymes) for hydrolysis of sugarcane bagasse. Feruloyl esterase plus xylanase increased 5.13-fold the releasing of ferulic acid from sugarcane bagasse. Removal of only 7.7% of ferulic acid content by AcFAE increased 97.3% the sugarcane bagasse hydrolysis by xylanase. These data support the use of AcFAE as an interesting adjuvant enzyme to improve lignocellulose digestion and biotechnological tool for biorefineries.

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