Screening of novel fungal Carbohydrate Esterase family 1 enzymes identifies three novel dual feruloyl/acetyl xylan esterases

Adiphol Dilokpimol; Bart Verkerk; Xinxin Li; Annie Bellemare; Mathieu Lavallee; Matthias Frommhagen; Emilie Nørmølle Underlin; Mirjam A. Kabel; Justin Powlowski; Adrian Tsang; Ronald P. de Vries

doi:10.1002/1873-3468.14322

Screening of novel fungal Carbohydrate Esterase family 1 enzymes identifies three novel dual feruloyl/acetyl xylan esterases

Adiphol Dilokpimol
, Bart Verkerk
, Xinxin Li
, Annie Bellemare
, Mathieu Lavallee
, Matthias Frommhagen
, Emilie Nørmølle Underlin
, Mirjam A. Kabel
, Justin Powlowski
, Adrian Tsang
, Ronald P. de Vries^*

^*Corresponding author for this work

Utrecht University
VTT Technical Research Centre of Finland Ltd.
Concordia University
Wageningen University & Research
Technical University of Denmark
Fungal Physiology, Westerdijk Fungal Biodiversity Institute and Fungal Molecular Physiology, Utrecht University, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands.

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

Abstract

Feruloyl esterases (FAEs) and acetyl xylan esterases (AXEs) are important enzymes for plant biomass degradation and are both present in Carbohydrate Esterase family 1 (CE1) of the Carbohydrate-Active enZymes database. In this study, ten novel fungal CE1 enzymes from different subfamilies were heterologously produced and screened for their activity towards model and complex plant biomass substrates. CE1_1 enzymes possess AXE activity, while CE1_5 enzymes showed FAE activity. Two enzymes from CE1_2 and one from CE1_5 possess dual feruloyl/acetyl xylan esterase (FXE) activity, showing expansion of substrate specificity. The new FXEs from CE1 can efficiently release both feruloyl and acetyl residues from feruloylated xylan, making them particularly interesting novel components of industrial enzyme cocktails for plant biomass degradation.

Original language	English
Pages (from-to)	1932-1943
Number of pages	12
Journal	FEBS Letters
Volume	596
Issue number	15
DOIs	https://doi.org/10.1002/1873-3468.14322
Publication status	Published - Aug 2022

Bibliographical note

Funding Information:
This work was supported by Genome Canada and Génome Québec. This work was partly supported by the China Scholarship Council to XL (grant no: 201803250066). The funding sources had no role in study design, in the collection, analysis and interpretation of data, in the writing of the manuscript, nor in the decision to submit the article for publication.

Publisher Copyright:
© 2022 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.

Funding

This work was supported by Genome Canada and Génome Québec. This work was partly supported by the China Scholarship Council to XL (grant no: 201803250066). The funding sources had no role in study design, in the collection, analysis and interpretation of data, in the writing of the manuscript, nor in the decision to submit the article for publication.

Keywords

acetyl xylan esterase
carbohydrate esterase family 1
feruloyl esterase
fungi
hydroxycinnamic acid
plant biomass

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FEBS Letters - 2022 - Dilokpimol - Screening of novel fungal Carbohydrate Esterase family 1 enzymes identifies three novelFinal published version, 1.59 MBLicence: CC BY-NC-ND

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title = "Screening of novel fungal Carbohydrate Esterase family 1 enzymes identifies three novel dual feruloyl/acetyl xylan esterases",

abstract = "Feruloyl esterases (FAEs) and acetyl xylan esterases (AXEs) are important enzymes for plant biomass degradation and are both present in Carbohydrate Esterase family 1 (CE1) of the Carbohydrate-Active enZymes database. In this study, ten novel fungal CE1 enzymes from different subfamilies were heterologously produced and screened for their activity towards model and complex plant biomass substrates. CE1\_1 enzymes possess AXE activity, while CE1\_5 enzymes showed FAE activity. Two enzymes from CE1\_2 and one from CE1\_5 possess dual feruloyl/acetyl xylan esterase (FXE) activity, showing expansion of substrate specificity. The new FXEs from CE1 can efficiently release both feruloyl and acetyl residues from feruloylated xylan, making them particularly interesting novel components of industrial enzyme cocktails for plant biomass degradation.",

keywords = "acetyl xylan esterase, carbohydrate esterase family 1, feruloyl esterase, fungi, hydroxycinnamic acid, plant biomass",

author = "Adiphol Dilokpimol and Bart Verkerk and Xinxin Li and Annie Bellemare and Mathieu Lavallee and Matthias Frommhagen and Underlin, \{Emilie N{\o}rm{\o}lle\} and Kabel, \{Mirjam A.\} and Justin Powlowski and Adrian Tsang and \{de Vries\}, \{Ronald P.\}",

note = "Funding Information: This work was supported by Genome Canada and G{\'e}nome Qu{\'e}bec. This work was partly supported by the China Scholarship Council to XL (grant no: 201803250066). The funding sources had no role in study design, in the collection, analysis and interpretation of data, in the writing of the manuscript, nor in the decision to submit the article for publication. Publisher Copyright: {\textcopyright} 2022 The Authors. FEBS Letters published by John Wiley \& Sons Ltd on behalf of Federation of European Biochemical Societies.",

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AU - Bellemare, Annie

AU - Lavallee, Mathieu

AU - Frommhagen, Matthias

AU - Underlin, Emilie Nørmølle

AU - Kabel, Mirjam A.

AU - Powlowski, Justin

AU - Tsang, Adrian

AU - de Vries, Ronald P.

N1 - Funding Information: This work was supported by Genome Canada and Génome Québec. This work was partly supported by the China Scholarship Council to XL (grant no: 201803250066). The funding sources had no role in study design, in the collection, analysis and interpretation of data, in the writing of the manuscript, nor in the decision to submit the article for publication. Publisher Copyright: © 2022 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.

PY - 2022/8

Y1 - 2022/8

N2 - Feruloyl esterases (FAEs) and acetyl xylan esterases (AXEs) are important enzymes for plant biomass degradation and are both present in Carbohydrate Esterase family 1 (CE1) of the Carbohydrate-Active enZymes database. In this study, ten novel fungal CE1 enzymes from different subfamilies were heterologously produced and screened for their activity towards model and complex plant biomass substrates. CE1_1 enzymes possess AXE activity, while CE1_5 enzymes showed FAE activity. Two enzymes from CE1_2 and one from CE1_5 possess dual feruloyl/acetyl xylan esterase (FXE) activity, showing expansion of substrate specificity. The new FXEs from CE1 can efficiently release both feruloyl and acetyl residues from feruloylated xylan, making them particularly interesting novel components of industrial enzyme cocktails for plant biomass degradation.

AB - Feruloyl esterases (FAEs) and acetyl xylan esterases (AXEs) are important enzymes for plant biomass degradation and are both present in Carbohydrate Esterase family 1 (CE1) of the Carbohydrate-Active enZymes database. In this study, ten novel fungal CE1 enzymes from different subfamilies were heterologously produced and screened for their activity towards model and complex plant biomass substrates. CE1_1 enzymes possess AXE activity, while CE1_5 enzymes showed FAE activity. Two enzymes from CE1_2 and one from CE1_5 possess dual feruloyl/acetyl xylan esterase (FXE) activity, showing expansion of substrate specificity. The new FXEs from CE1 can efficiently release both feruloyl and acetyl residues from feruloylated xylan, making them particularly interesting novel components of industrial enzyme cocktails for plant biomass degradation.

KW - acetyl xylan esterase

KW - carbohydrate esterase family 1

KW - feruloyl esterase

KW - fungi

KW - hydroxycinnamic acid

KW - plant biomass

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Screening of novel fungal Carbohydrate Esterase family 1 enzymes identifies three novel dual feruloyl/acetyl xylan esterases

Abstract

Bibliographical note

Funding

Keywords

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