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

TY - JOUR

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

AU - Dilokpimol, Adiphol

AU - Makela, Miia R.

AU - Varriale, Simona

AU - Zhou, Miaomiao

AU - Cerullo, Gabriella

AU - Gidijala, Loknath

AU - Hinkka, Harri

AU - Bras, Joana L. A.

AU - Juetten, Peter

AU - Piechot, Alexander

AU - Verhaert, Raymond

AU - Hilden, Kristiina S.

AU - Faraco, Vincenza

AU - de Vries, Ronald P.

N1 - Copyright © 2017 Elsevier B.V. All rights reserved.

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 - Feruloyl esterase

KW - Ferulic acid

KW - Genome mining

KW - Plant cell wall

KW - Fungi

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 -