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Multifunctional cellulases are potent, versatile tools for a renewable bioeconomy

Enzyme performance is critical to the future bioeconomy based on renewable plant materials. Plant biomass can be efficiently hydrolyzed by multifunctional cellulases (MFCs) into sugars suitable for conversion into fuels and chemicals, and MFCs fall into three functional categories. Recent work revea...

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Detalles Bibliográficos
Autores principales: Glasgow, Evan, Meulen, Kirk Vander, Kuch, Nate, Fox, Brian G
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8366578/
https://www.ncbi.nlm.nih.gov/pubmed/33550093
http://dx.doi.org/10.1016/j.copbio.2020.12.020
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author Glasgow, Evan
Meulen, Kirk Vander
Kuch, Nate
Fox, Brian G
author_facet Glasgow, Evan
Meulen, Kirk Vander
Kuch, Nate
Fox, Brian G
author_sort Glasgow, Evan
collection PubMed
description Enzyme performance is critical to the future bioeconomy based on renewable plant materials. Plant biomass can be efficiently hydrolyzed by multifunctional cellulases (MFCs) into sugars suitable for conversion into fuels and chemicals, and MFCs fall into three functional categories. Recent work revealed MFCs with broad substrate specificity, dual exo-activity/endo-activity on cellulose, and intramolecular synergy, among other novel characteristics. Binding modules and accessory catalytic domains amplify MFC and xylanase activity in a wide variety of ways, and processive endoglucanases achieve autosynergy on cellulose. Multidomain MFCs from Caldicellulosiruptor are heat-tolerant, adaptable to variable cellulose crystallinity, and may provide interchangeable scaffolds for recombinant design. Further studies of MFC properties and their reactivity with plant biomass are recommended for increasing biorefinery yields.
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spelling pubmed-83665782022-02-04 Multifunctional cellulases are potent, versatile tools for a renewable bioeconomy Glasgow, Evan Meulen, Kirk Vander Kuch, Nate Fox, Brian G Curr Opin Biotechnol Article Enzyme performance is critical to the future bioeconomy based on renewable plant materials. Plant biomass can be efficiently hydrolyzed by multifunctional cellulases (MFCs) into sugars suitable for conversion into fuels and chemicals, and MFCs fall into three functional categories. Recent work revealed MFCs with broad substrate specificity, dual exo-activity/endo-activity on cellulose, and intramolecular synergy, among other novel characteristics. Binding modules and accessory catalytic domains amplify MFC and xylanase activity in a wide variety of ways, and processive endoglucanases achieve autosynergy on cellulose. Multidomain MFCs from Caldicellulosiruptor are heat-tolerant, adaptable to variable cellulose crystallinity, and may provide interchangeable scaffolds for recombinant design. Further studies of MFC properties and their reactivity with plant biomass are recommended for increasing biorefinery yields. 2021-02-04 2021-02 /pmc/articles/PMC8366578/ /pubmed/33550093 http://dx.doi.org/10.1016/j.copbio.2020.12.020 Text en https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/) ).
spellingShingle Article
Glasgow, Evan
Meulen, Kirk Vander
Kuch, Nate
Fox, Brian G
Multifunctional cellulases are potent, versatile tools for a renewable bioeconomy
title Multifunctional cellulases are potent, versatile tools for a renewable bioeconomy
title_full Multifunctional cellulases are potent, versatile tools for a renewable bioeconomy
title_fullStr Multifunctional cellulases are potent, versatile tools for a renewable bioeconomy
title_full_unstemmed Multifunctional cellulases are potent, versatile tools for a renewable bioeconomy
title_short Multifunctional cellulases are potent, versatile tools for a renewable bioeconomy
title_sort multifunctional cellulases are potent, versatile tools for a renewable bioeconomy
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8366578/
https://www.ncbi.nlm.nih.gov/pubmed/33550093
http://dx.doi.org/10.1016/j.copbio.2020.12.020
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