Characterization of a feruloyl esterase from Aspergillus terreus facilitates the division of fungal enzymes from Carbohydrate Esterase family 1 of the carbohydrate-active enzymes (CAZy) database

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Mäkelä , M R , Dilokpimol , A , Koskela , S M , Kuuskeri , J , de Vries , R P & Hilden , K 2018 , ' Characterization of a feruloyl esterase from Aspergillus terreus facilitates the division of fungal enzymes from Carbohydrate Esterase family 1 of the carbohydrate-active enzymes (CAZy) database ' , Microbial Biotechnology , vol. 11 , no. 5 , pp. 869-880 . https://doi.org/10.1111/1751-7915.13273

Title: Characterization of a feruloyl esterase from Aspergillus terreus facilitates the division of fungal enzymes from Carbohydrate Esterase family 1 of the carbohydrate-active enzymes (CAZy) database
Author: Mäkelä, Miia R.; Dilokpimol, Adiphol; Koskela, Salla M.; Kuuskeri, Jaana; de Vries, Ronald P.; Hilden, Kristiina
Contributor: University of Helsinki, Department of Microbiology
University of Helsinki, Department of Microbiology
University of Helsinki, Department of Microbiology
University of Helsinki, Helsinki Institute of Sustainability Science (HELSUS)
Date: 2018-09
Language: eng
Number of pages: 12
Belongs to series: Microbial Biotechnology
ISSN: 1751-7915
URI: http://hdl.handle.net/10138/241224
Abstract: Feruloyl esterases (FAEs) are accessory enzymes for plant biomass degradation, which catalyse hydrolysis of carboxylic ester linkages between hydroxycinnamic acids and plant cell-wall carbohydrates. They are a diverse group of enzymes evolved from, e.g. acetyl xylan esterases (AXEs), lipases and tannases, thus complicating their classification and prediction of function by sequence similarity. Recently, an increasing number of fungal FAEs have been biochemically characterized, owing to their potential in various biotechnological applications and multitude of candidate FAEs in fungal genomes. However, only part of the fungal FAEs are included in Carbohydrate Esterase family 1 (CE1) of the carbohydrate-active enzymes (CAZy) database. In this work, we performed a phylogenetic analysis that divided the fungal members of CE1 into five subfamilies of which three contained characterized enzymes with conserved activities. Conservation within one of the subfamilies was confirmed by characterization of an additional CE1 enzyme from Aspergillus terreus. Recombinant A.terreus FaeD (AtFaeD) showed broad specificity towards synthetic methyl and ethyl esters, and released ferulic acid from plant biomass substrates, demonstrating its true FAE activity and interesting features as potential biocatalyst. The subfamily division of the fungal CE1 members enables more efficient selection of candidate enzymes for biotechnological processes.
Subject: ACETYL XYLAN ESTERASE
PLANT-CELL WALLS
METHYL PHENYLALKANOATES
SUBSTRATE-SPECIFICITY
BIOMASS DEGRADATION
MOLECULAR-CLONING
PICHIA-PASTORIS
BINDING MODULE
ACID
GENE
1183 Plant biology, microbiology, virology
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