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Diversity of fungal feruloyl esterases: updated phylogenetic classification, properties, and industrial applications
Feruloyl esterases (FAEs) represent a diverse group of carboxyl esterases that specifically catalyze the hydrolysis of ester bonds between ferulic (hydroxycinnamic) acid and plant cell wall polysaccharides. Therefore, FAEs act as accessory enzymes to assist xylanolytic and pectinolytic enzymes in ga...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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BioMed Central
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5084320/ https://www.ncbi.nlm.nih.gov/pubmed/27795736 http://dx.doi.org/10.1186/s13068-016-0651-6 |
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author | Dilokpimol, Adiphol Mäkelä, Miia R. Aguilar-Pontes, Maria Victoria Benoit-Gelber, Isabelle Hildén, Kristiina S. de Vries, Ronald P. |
author_facet | Dilokpimol, Adiphol Mäkelä, Miia R. Aguilar-Pontes, Maria Victoria Benoit-Gelber, Isabelle Hildén, Kristiina S. de Vries, Ronald P. |
author_sort | Dilokpimol, Adiphol |
collection | PubMed |
description | Feruloyl esterases (FAEs) represent a diverse group of carboxyl esterases that specifically catalyze the hydrolysis of ester bonds between ferulic (hydroxycinnamic) acid and plant cell wall polysaccharides. Therefore, FAEs act as accessory enzymes to assist xylanolytic and pectinolytic enzymes in gaining access to their site of action during biomass conversion. Their ability to release ferulic acid and other hydroxycinnamic acids from plant biomass makes FAEs potential biocatalysts in a wide variety of applications such as in biofuel, food and feed, pulp and paper, cosmetics, and pharmaceutical industries. This review provides an updated overview of the knowledge on fungal FAEs, in particular describing their role in plant biomass degradation, diversity of their biochemical properties and substrate specificities, their regulation and conditions needed for their induction. Furthermore, the discovery of new FAEs using genome mining and phylogenetic analysis of current publicly accessible fungal genomes will also be presented. This has led to a new subfamily classification of fungal FAEs that takes into account both phylogeny and substrate specificity. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13068-016-0651-6) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-5084320 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-50843202016-10-28 Diversity of fungal feruloyl esterases: updated phylogenetic classification, properties, and industrial applications Dilokpimol, Adiphol Mäkelä, Miia R. Aguilar-Pontes, Maria Victoria Benoit-Gelber, Isabelle Hildén, Kristiina S. de Vries, Ronald P. Biotechnol Biofuels Review Feruloyl esterases (FAEs) represent a diverse group of carboxyl esterases that specifically catalyze the hydrolysis of ester bonds between ferulic (hydroxycinnamic) acid and plant cell wall polysaccharides. Therefore, FAEs act as accessory enzymes to assist xylanolytic and pectinolytic enzymes in gaining access to their site of action during biomass conversion. Their ability to release ferulic acid and other hydroxycinnamic acids from plant biomass makes FAEs potential biocatalysts in a wide variety of applications such as in biofuel, food and feed, pulp and paper, cosmetics, and pharmaceutical industries. This review provides an updated overview of the knowledge on fungal FAEs, in particular describing their role in plant biomass degradation, diversity of their biochemical properties and substrate specificities, their regulation and conditions needed for their induction. Furthermore, the discovery of new FAEs using genome mining and phylogenetic analysis of current publicly accessible fungal genomes will also be presented. This has led to a new subfamily classification of fungal FAEs that takes into account both phylogeny and substrate specificity. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13068-016-0651-6) contains supplementary material, which is available to authorized users. BioMed Central 2016-10-28 /pmc/articles/PMC5084320/ /pubmed/27795736 http://dx.doi.org/10.1186/s13068-016-0651-6 Text en © The Author(s) 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Review Dilokpimol, Adiphol Mäkelä, Miia R. Aguilar-Pontes, Maria Victoria Benoit-Gelber, Isabelle Hildén, Kristiina S. de Vries, Ronald P. Diversity of fungal feruloyl esterases: updated phylogenetic classification, properties, and industrial applications |
title | Diversity of fungal feruloyl esterases: updated phylogenetic classification, properties, and industrial applications |
title_full | Diversity of fungal feruloyl esterases: updated phylogenetic classification, properties, and industrial applications |
title_fullStr | Diversity of fungal feruloyl esterases: updated phylogenetic classification, properties, and industrial applications |
title_full_unstemmed | Diversity of fungal feruloyl esterases: updated phylogenetic classification, properties, and industrial applications |
title_short | Diversity of fungal feruloyl esterases: updated phylogenetic classification, properties, and industrial applications |
title_sort | diversity of fungal feruloyl esterases: updated phylogenetic classification, properties, and industrial applications |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5084320/ https://www.ncbi.nlm.nih.gov/pubmed/27795736 http://dx.doi.org/10.1186/s13068-016-0651-6 |
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