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

doi:10.1007/s12010-007-8074-2

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

National Renewable Energy Laboratory

Research output: Contribution to journal › Article › peer-review

17 Scopus Citations

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.

Original language	American English
Pages (from-to)	79-87
Number of pages	9
Journal	Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology
Volume	146
Issue number	1-3
DOIs	https://doi.org/10.1007/s12010-007-8074-2 https://doi.org/10.1007/s12010-007-8074-2
State	Published - 2008

NREL Publication Number

NREL/JA-510-43379

Keywords

Biomass digestion
Cellulose
Ferulic acid esterase
Hemicellulose
Heterologous expression

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title = "Heterologous Expression of Two Ferulic Acid Esterases from Penicillium Funiculosum",

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.",

keywords = "Biomass digestion, Cellulose, Ferulic acid esterase, Hemicellulose, Heterologous expression",

author = "Knoshaug, {Eric P.} and Selig, {Michael J.} and Baker, {John O.} and Decker, {Stephen R.} and Himmel, {Michael E.} and Adney, {William S.}",

year = "2008",

doi = "10.1007/s12010-007-8074-2",

language = "American English",

volume = "146",

pages = "79--87",

journal = "Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology",

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T1 - Heterologous Expression of Two Ferulic Acid Esterases from Penicillium Funiculosum

AU - Knoshaug, Eric P.

AU - Selig, Michael J.

AU - Baker, John O.

AU - Decker, Stephen R.

AU - Himmel, Michael E.

AU - Adney, William S.

PY - 2008

Y1 - 2008

N2 - 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.

AB - 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.

KW - Biomass digestion

KW - Cellulose

KW - Ferulic acid esterase

KW - Hemicellulose

KW - Heterologous expression

UR - http://www.scopus.com/inward/record.url?scp=49349099268&partnerID=8YFLogxK

U2 - 10.1007/s12010-007-8074-2

DO - 10.1007/s12010-007-8074-2

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SN - 0273-2289

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EP - 87

JO - Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology

JF - Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology

IS - 1-3

ER -

Heterologous Expression of Two Ferulic Acid Esterases from Penicillium Funiculosum

Abstract

NREL Publication Number

Keywords

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