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

Adiphol Dilokpimol, Miia R. Makela, Simona Varriale, Miaomiao Zhou, Gabriella Cerullo, Loknath Gidijala, Harri Hinkka, Joana L. A. Bras, Peter Juetten, Alexander Piechot, Raymond Verhaert, Kristiina S. Hilden, Vincenza Faraco, Ronald P. de Vries

Onderzoeksoutput: Bijdrage aan wetenschappelijk tijdschrift/periodieke uitgaveArtikelWetenschappelijkpeer review

Samenvatting

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.

Originele taal-2Engels
Pagina's (van-tot)9-14
Aantal pagina's6
TijdschriftNew Biotechnology
Volume41
Vroegere onlinedatum23 nov. 2017
DOI's
StatusGepubliceerd - 25 mrt. 2018

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