Fungal feruloyl esterases: Functional validation of genome mining based enzyme discovery including uncharacterized subfamilies

Adiphol Dilokpimol; Miia R. Mäkelä; Simona Varriale; Miaomiao Zhou; Gabriella Cerullo; Loknath Gidijala; Harri Hinkka; Joana L A Brás; Peter Jütten; Alexander Piechot; Raymond Verhaert; Kristiina S. Hildén; Vincenza Faraco; Ronald P. de Vries

doi:10.1016/j.nbt.2017.11.004

Fungal feruloyl esterases: Functional validation of genome mining based enzyme discovery including uncharacterized subfamilies

Adiphol Dilokpimol
, Miia R. Mäkelä
, Simona Varriale
, Miaomiao Zhou
, Gabriella Cerullo
, Loknath Gidijala
, Harri Hinkka
, Joana L A Brás
, Peter Jütten
, Alexander Piechot
, Raymond Verhaert
, Kristiina S. Hildén^*
, Vincenza Faraco^*
, Ronald P. de Vries^*

^*Corresponding author for this work

Not published at VTT

Utrecht University
University of Helsinki
University of Naples Federico II
ProteoNic B.V.
NZYTech B.V.
Taros Chemicals GmbH & Co KG

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

31 Citations (Scopus)

Abstract

Feruloyl esterases (FAEs) are a diverse group of enzymes that specifically catalyze the hydrolysis of ester bonds between a hydroxycinnamic (e.g. ferulic) acid and plant poly- or oligosaccharides. FAEs as auxiliary enzymes significantly assist xylanolytic and pectinolytic enzymes in gaining access to their site of action during biomass saccharification for biofuel and biochemical production. A limited number of FAEs have been functionally characterized compared to over 1000 putative fungal FAEs that were recently predicted by similarity-based genome mining, which divided phylogenetically into different subfamilies (SFs). In this study, 27 putative and six characterized FAEs from both ascomycete and basidiomycete fungi were selected and heterologously expressed in Pichia pastoris and the recombinant proteins biochemically characterized to validate the previous genome mining and phylogenetical grouping and to expand the information on activity of fungal FAEs. As a result, 20 enzymes were shown to possess FAE activity, being active towards pNP-ferulate and/or methyl hydroxycinnamate substrates, and covering 11 subfamilies. Most of the new FAEs showed activities comparable to those of previously characterized fungal FAEs.

Original language	English
Pages (from-to)	9-14
Journal	New Biotechnology
Volume	41
DOIs	https://doi.org/10.1016/j.nbt.2017.11.004
Publication status	Published - 25 Mar 2018
MoE publication type	A1 Journal article-refereed

Funding

This work was supported by the European Union , Grant agreement no: 613868 (OPTIBIOCAT).

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 7 Affordable and Clean Energy

Keywords

Ferulic acid
Feruloyl esterase
Fungi
Genome mining
Plant cell wall

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10.1016/j.nbt.2017.11.004Licence: CC BY-NC-ND

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Dilokpimol, A., Mäkelä, M. R., Varriale, S., Zhou, M., Cerullo, G., Gidijala, L., Hinkka, H., Brás, J. L. A., Jütten, P., Piechot, A., Verhaert, R., Hildén, K. S., Faraco, V., & de Vries, R. P. (2018). Fungal feruloyl esterases: Functional validation of genome mining based enzyme discovery including uncharacterized subfamilies. New Biotechnology, 41, 9-14. https://doi.org/10.1016/j.nbt.2017.11.004

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title = "Fungal feruloyl esterases: Functional validation of genome mining based enzyme discovery including uncharacterized subfamilies",

abstract = "Feruloyl esterases (FAEs) are a diverse group of enzymes that specifically catalyze the hydrolysis of ester bonds between a hydroxycinnamic (e.g. ferulic) acid and plant poly- or oligosaccharides. FAEs as auxiliary enzymes significantly assist xylanolytic and pectinolytic enzymes in gaining access to their site of action during biomass saccharification for biofuel and biochemical production. A limited number of FAEs have been functionally characterized compared to over 1000 putative fungal FAEs that were recently predicted by similarity-based genome mining, which divided phylogenetically into different subfamilies (SFs). In this study, 27 putative and six characterized FAEs from both ascomycete and basidiomycete fungi were selected and heterologously expressed in Pichia pastoris and the recombinant proteins biochemically characterized to validate the previous genome mining and phylogenetical grouping and to expand the information on activity of fungal FAEs. As a result, 20 enzymes were shown to possess FAE activity, being active towards pNP-ferulate and/or methyl hydroxycinnamate substrates, and covering 11 subfamilies. Most of the new FAEs showed activities comparable to those of previously characterized fungal FAEs.",

keywords = "Ferulic acid, Feruloyl esterase, Fungi, Genome mining, Plant cell wall",

author = "Adiphol Dilokpimol and M{\"a}kel{\"a}, \{Miia R.\} and Simona Varriale and Miaomiao Zhou and Gabriella Cerullo and Loknath Gidijala and Harri Hinkka and Br{\'a}s, \{Joana L A\} and Peter J{\"u}tten and Alexander Piechot and Raymond Verhaert and Hild{\'e}n, \{Kristiina S.\} and Vincenza Faraco and \{de Vries\}, \{Ronald P.\}",

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year = "2018",

month = mar,

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doi = "10.1016/j.nbt.2017.11.004",

language = "English",

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Dilokpimol, A, Mäkelä, MR, Varriale, S, Zhou, M, Cerullo, G, Gidijala, L, Hinkka, H, Brás, JLA, Jütten, P, Piechot, A, Verhaert, R, Hildén, KS, Faraco, V & de Vries, RP 2018, 'Fungal feruloyl esterases: Functional validation of genome mining based enzyme discovery including uncharacterized subfamilies', New Biotechnology, vol. 41, pp. 9-14. https://doi.org/10.1016/j.nbt.2017.11.004

TY - JOUR

T1 - Fungal feruloyl esterases

T2 - Functional validation of genome mining based enzyme discovery including uncharacterized subfamilies

AU - Dilokpimol, Adiphol

AU - Mäkelä, Miia R.

AU - Varriale, Simona

AU - Zhou, Miaomiao

AU - Cerullo, Gabriella

AU - Gidijala, Loknath

AU - Hinkka, Harri

AU - Brás, Joana L A

AU - Jütten, Peter

AU - Piechot, Alexander

AU - Verhaert, Raymond

AU - Hildén, Kristiina S.

AU - Faraco, Vincenza

AU - de Vries, Ronald P.

PY - 2018/3/25

Y1 - 2018/3/25

N2 - Feruloyl esterases (FAEs) are a diverse group of enzymes that specifically catalyze the hydrolysis of ester bonds between a hydroxycinnamic (e.g. ferulic) acid and plant poly- or oligosaccharides. FAEs as auxiliary enzymes significantly assist xylanolytic and pectinolytic enzymes in gaining access to their site of action during biomass saccharification for biofuel and biochemical production. A limited number of FAEs have been functionally characterized compared to over 1000 putative fungal FAEs that were recently predicted by similarity-based genome mining, which divided phylogenetically into different subfamilies (SFs). In this study, 27 putative and six characterized FAEs from both ascomycete and basidiomycete fungi were selected and heterologously expressed in Pichia pastoris and the recombinant proteins biochemically characterized to validate the previous genome mining and phylogenetical grouping and to expand the information on activity of fungal FAEs. As a result, 20 enzymes were shown to possess FAE activity, being active towards pNP-ferulate and/or methyl hydroxycinnamate substrates, and covering 11 subfamilies. Most of the new FAEs showed activities comparable to those of previously characterized fungal FAEs.

AB - Feruloyl esterases (FAEs) are a diverse group of enzymes that specifically catalyze the hydrolysis of ester bonds between a hydroxycinnamic (e.g. ferulic) acid and plant poly- or oligosaccharides. FAEs as auxiliary enzymes significantly assist xylanolytic and pectinolytic enzymes in gaining access to their site of action during biomass saccharification for biofuel and biochemical production. A limited number of FAEs have been functionally characterized compared to over 1000 putative fungal FAEs that were recently predicted by similarity-based genome mining, which divided phylogenetically into different subfamilies (SFs). In this study, 27 putative and six characterized FAEs from both ascomycete and basidiomycete fungi were selected and heterologously expressed in Pichia pastoris and the recombinant proteins biochemically characterized to validate the previous genome mining and phylogenetical grouping and to expand the information on activity of fungal FAEs. As a result, 20 enzymes were shown to possess FAE activity, being active towards pNP-ferulate and/or methyl hydroxycinnamate substrates, and covering 11 subfamilies. Most of the new FAEs showed activities comparable to those of previously characterized fungal FAEs.

KW - Ferulic acid

KW - Feruloyl esterase

KW - Fungi

KW - Genome mining

KW - Plant cell wall

UR - https://www.scopus.com/pages/publications/85034847672

U2 - 10.1016/j.nbt.2017.11.004

DO - 10.1016/j.nbt.2017.11.004

M3 - Article

C2 - 29174720

SN - 1871-6784

VL - 41

SP - 9

EP - 14

JO - New Biotechnology

JF - New Biotechnology

ER -

Fungal feruloyl esterases: Functional validation of genome mining based enzyme discovery including uncharacterized subfamilies

Abstract

Funding

UN SDGs

Keywords

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