Fungal glucuronoyl esterases: Genome mining based enzyme discovery and biochemical characterization

TY - JOUR

T1 - Fungal glucuronoyl esterases

T2 - Genome mining based enzyme discovery and biochemical characterization

AU - Dilokpimol, Adiphol

AU - Mäkelä, Miia R

AU - Cerullo, Gabriella

AU - Zhou, Miaomiao

AU - Varriale, Simona

AU - Gidijala, Loknath

AU - Brás, Joana L A

AU - Jütten, Peter

AU - Piechot, Alexander

AU - Verhaert, Raymond

AU - Faraco, Vincenza

AU - Hilden, Kristiina S.

AU - de Vries, Ronald P

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

PY - 2018/1/25

Y1 - 2018/1/25

N2 - 4-O-Methyl-d-glucuronic acid (MeGlcA) is a side-residue of glucuronoarabinoxylan and can form ester linkages to lignin, contributing significantly to the strength and rigidity of the plant cell wall. Glucuronoyl esterases (4-O-methyl-glucuronoyl methylesterases, GEs) can cleave this ester bond, and therefore may play a significant role as auxiliary enzymes in biomass saccharification for the production of biofuels and biochemicals. GEs belong to a relatively new family of carbohydrate esterases (CE15) in the CAZy database (www.cazy.org), and so far around ten fungal GEs have been characterized. To explore additional GE enzymes, we used a genome mining strategy. BLAST analysis with characterized GEs against approximately 250 publicly accessible fungal genomes identified more than 150 putative fungal GEs, which were classified into eight phylogenetic sub-groups. To validate the genome mining strategy, 21 selected GEs from both ascomycete and basidiomycete fungi were heterologously produced in Pichia pastoris. Of these enzymes, 18 were active against benzyl d-glucuronate demonstrating the suitability of our genome mining strategy for enzyme discovery.

AB - 4-O-Methyl-d-glucuronic acid (MeGlcA) is a side-residue of glucuronoarabinoxylan and can form ester linkages to lignin, contributing significantly to the strength and rigidity of the plant cell wall. Glucuronoyl esterases (4-O-methyl-glucuronoyl methylesterases, GEs) can cleave this ester bond, and therefore may play a significant role as auxiliary enzymes in biomass saccharification for the production of biofuels and biochemicals. GEs belong to a relatively new family of carbohydrate esterases (CE15) in the CAZy database (www.cazy.org), and so far around ten fungal GEs have been characterized. To explore additional GE enzymes, we used a genome mining strategy. BLAST analysis with characterized GEs against approximately 250 publicly accessible fungal genomes identified more than 150 putative fungal GEs, which were classified into eight phylogenetic sub-groups. To validate the genome mining strategy, 21 selected GEs from both ascomycete and basidiomycete fungi were heterologously produced in Pichia pastoris. Of these enzymes, 18 were active against benzyl d-glucuronate demonstrating the suitability of our genome mining strategy for enzyme discovery.

KW - Journal Article

U2 - 10.1016/j.nbt.2017.10.003

DO - 10.1016/j.nbt.2017.10.003

M3 - Article

C2 - 29051046

SN - 1871-6784

VL - 40

SP - 282

EP - 287

JO - New Biotechnology

JF - New Biotechnology

IS - Pt B

ER -