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

Adiphol Dilokpimol, Miia Riitta Mäkelä, Simona Varriale, Miaomiao Zhou, Gabriella Cerullo, Loknath Gidijala, Harri Tapio Hinkka, Joana L.A. Brás, Peter Jütten, Alexander Piechot, Raymond Verhaert, Sari Kristiina Hilden, Vincenza Faraco, Ronald de Vries

Research output: Contribution to journalArticleScientificpeer-review

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 languageEnglish
JournalNew Biotechnology
Volume41
Pages (from-to)9-14
Number of pages6
ISSN1871-6784
DOIs
Publication statusPublished - 2018
MoE publication typeA1 Journal article-refereed

Fields of Science

  • 1182 Biochemistry, cell and molecular biology
  • Feruloyl esterase
  • Ferulic acid
  • Genome mining
  • Plant cell wall
  • Fungi
  • CELL WALL POLYSACCHARIDES
  • ASPERGILLUS-NIGER
  • CRYSTAL-STRUCTURE
  • ACID
  • DEGRADATION
  • FAMILY
  • OLIGOSACCHARIDES
  • PURIFICATION
  • SPECIFICITY
  • PERFORMANCE

Cite this

Dilokpimol, Adiphol ; Mäkelä, Miia Riitta ; Varriale, Simona ; Zhou, Miaomiao ; Cerullo, Gabriella ; Gidijala, Loknath ; Hinkka, Harri Tapio ; Brás, Joana L.A. ; Jütten, Peter ; Piechot, Alexander ; Verhaert, Raymond ; Hilden, Sari Kristiina ; Faraco, Vincenza ; de Vries, Ronald. / Fungal feruloyl esterases: Functional validation of genome mining based enzyme discovery including uncharacterized subfamilies. In: New Biotechnology. 2018 ; Vol. 41. pp. 9-14.
@article{e5465170987747e3ac7417233c279080,
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 = "1182 Biochemistry, cell and molecular biology, Feruloyl esterase, Ferulic acid, Genome mining, Plant cell wall, Fungi, CELL WALL POLYSACCHARIDES, ASPERGILLUS-NIGER, CRYSTAL-STRUCTURE, ACID, DEGRADATION, FAMILY, OLIGOSACCHARIDES, PURIFICATION, SPECIFICITY, PERFORMANCE",
author = "Adiphol Dilokpimol and M{\"a}kel{\"a}, {Miia Riitta} and Simona Varriale and Miaomiao Zhou and Gabriella Cerullo and Loknath Gidijala and Hinkka, {Harri Tapio} and Br{\'a}s, {Joana L.A.} and Peter J{\"u}tten and Alexander Piechot and Raymond Verhaert and Hilden, {Sari Kristiina} and Vincenza Faraco and {de Vries}, Ronald",
year = "2018",
doi = "10.1016/j.nbt.2017.11.004",
language = "English",
volume = "41",
pages = "9--14",
journal = "New Biotechnology",
issn = "1871-6784",
publisher = "Elsevier Scientific Publ. Co",

}

Dilokpimol, A, Mäkelä, MR, Varriale, S, Zhou, M, Cerullo, G, Gidijala, L, Hinkka, HT, Brás, JLA, Jütten, P, Piechot, A, Verhaert, R, Hilden, SK, Faraco, V & de Vries, R 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

Fungal feruloyl esterases: Functional validation of genome mining based enzyme discovery including uncharacterized subfamilies. / Dilokpimol, Adiphol; Mäkelä, Miia Riitta; Varriale, Simona; Zhou, Miaomiao; Cerullo, Gabriella ; Gidijala, Loknath ; Hinkka, Harri Tapio; Brás, Joana L.A. ; Jütten, Peter; Piechot, Alexander ; Verhaert, Raymond ; Hilden, Sari Kristiina; Faraco, Vincenza ; de Vries, Ronald.

In: New Biotechnology, Vol. 41, 2018, p. 9-14.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Fungal feruloyl esterases: Functional validation of genome mining based enzyme discovery including uncharacterized subfamilies

AU - Dilokpimol, Adiphol

AU - Mäkelä, Miia Riitta

AU - Varriale, Simona

AU - Zhou, Miaomiao

AU - Cerullo, Gabriella

AU - Gidijala, Loknath

AU - Hinkka, Harri Tapio

AU - Brás, Joana L.A.

AU - Jütten, Peter

AU - Piechot, Alexander

AU - Verhaert, Raymond

AU - Hilden, Sari Kristiina

AU - Faraco, Vincenza

AU - de Vries, Ronald

PY - 2018

Y1 - 2018

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 - 1182 Biochemistry, cell and molecular biology

KW - Feruloyl esterase

KW - Ferulic acid

KW - Genome mining

KW - Plant cell wall

KW - Fungi

KW - CELL WALL POLYSACCHARIDES

KW - ASPERGILLUS-NIGER

KW - CRYSTAL-STRUCTURE

KW - ACID

KW - DEGRADATION

KW - FAMILY

KW - OLIGOSACCHARIDES

KW - PURIFICATION

KW - SPECIFICITY

KW - PERFORMANCE

U2 - 10.1016/j.nbt.2017.11.004

DO - 10.1016/j.nbt.2017.11.004

M3 - Article

VL - 41

SP - 9

EP - 14

JO - New Biotechnology

JF - New Biotechnology

SN - 1871-6784

ER -