A novel fungal metal-dependent α-l-arabinofuranosidase of family 54 glycoside hydrolase shows expanded substrate specificity

Abstract Trichoderma genus fungi present great potential for the production of carbohydrate-active enzymes (CAZYmes), including glycoside hydrolase (GH) family members. From a renewability perspective, CAZYmes can be biotechnologically exploited to convert plant biomass into free sugars for the prod...

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Autores principales:	Maria Lorenza Leal Motta, Jaire Alves Ferreira Filho, Ricardo Rodrigues de Melo, Leticia Maria Zanphorlin, Clelton Aparecido dos Santos, Anete Pereira de Souza
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0bb66bb4d5704a35bd1e0cb8f436517a
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spelling	oai:doaj.org-article:0bb66bb4d5704a35bd1e0cb8f436517a2021-12-02T14:49:11ZA novel fungal metal-dependent α-l-arabinofuranosidase of family 54 glycoside hydrolase shows expanded substrate specificity10.1038/s41598-021-90490-22045-2322https://doaj.org/article/0bb66bb4d5704a35bd1e0cb8f436517a2021-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-90490-2https://doaj.org/toc/2045-2322Abstract Trichoderma genus fungi present great potential for the production of carbohydrate-active enzymes (CAZYmes), including glycoside hydrolase (GH) family members. From a renewability perspective, CAZYmes can be biotechnologically exploited to convert plant biomass into free sugars for the production of advanced biofuels and other high-value chemicals. GH54 is an attractive enzyme family for biotechnological applications because many GH54 enzymes are bifunctional. Thus, GH54 enzymes are interesting targets in the search for new enzymes for use in industrial processes such as plant biomass conversion. Herein, a novel metal-dependent GH54 arabinofuranosidase (ThABF) from the cellulolytic fungus Trichoderma harzianum was identified and biochemically characterized. Initial in silico searches were performed to identify the GH54 sequence. Next, the gene was cloned and heterologously overexpressed in Escherichia coli. The recombinant protein was purified, and the enzyme’s biochemical and biophysical properties were assessed. GH54 members show wide functional diversity and specifically remove plant cell substitutions including arabinose and galactose in the presence of a metallic cofactor. Plant cell wall substitution has a major impact on lignocellulosic substrate conversion into high-value chemicals. These results expand the known functional diversity of the GH54 family, showing the potential of a novel arabinofuranosidase for plant biomass degradation.Maria Lorenza Leal MottaJaire Alves Ferreira FilhoRicardo Rodrigues de MeloLeticia Maria ZanphorlinClelton Aparecido dos SantosAnete Pereira de SouzaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Maria Lorenza Leal Motta Jaire Alves Ferreira Filho Ricardo Rodrigues de Melo Leticia Maria Zanphorlin Clelton Aparecido dos Santos Anete Pereira de Souza A novel fungal metal-dependent α-l-arabinofuranosidase of family 54 glycoside hydrolase shows expanded substrate specificity
description	Abstract Trichoderma genus fungi present great potential for the production of carbohydrate-active enzymes (CAZYmes), including glycoside hydrolase (GH) family members. From a renewability perspective, CAZYmes can be biotechnologically exploited to convert plant biomass into free sugars for the production of advanced biofuels and other high-value chemicals. GH54 is an attractive enzyme family for biotechnological applications because many GH54 enzymes are bifunctional. Thus, GH54 enzymes are interesting targets in the search for new enzymes for use in industrial processes such as plant biomass conversion. Herein, a novel metal-dependent GH54 arabinofuranosidase (ThABF) from the cellulolytic fungus Trichoderma harzianum was identified and biochemically characterized. Initial in silico searches were performed to identify the GH54 sequence. Next, the gene was cloned and heterologously overexpressed in Escherichia coli. The recombinant protein was purified, and the enzyme’s biochemical and biophysical properties were assessed. GH54 members show wide functional diversity and specifically remove plant cell substitutions including arabinose and galactose in the presence of a metallic cofactor. Plant cell wall substitution has a major impact on lignocellulosic substrate conversion into high-value chemicals. These results expand the known functional diversity of the GH54 family, showing the potential of a novel arabinofuranosidase for plant biomass degradation.
format	article
author	Maria Lorenza Leal Motta Jaire Alves Ferreira Filho Ricardo Rodrigues de Melo Leticia Maria Zanphorlin Clelton Aparecido dos Santos Anete Pereira de Souza
author_facet	Maria Lorenza Leal Motta Jaire Alves Ferreira Filho Ricardo Rodrigues de Melo Leticia Maria Zanphorlin Clelton Aparecido dos Santos Anete Pereira de Souza
author_sort	Maria Lorenza Leal Motta
title	A novel fungal metal-dependent α-l-arabinofuranosidase of family 54 glycoside hydrolase shows expanded substrate specificity
title_short	A novel fungal metal-dependent α-l-arabinofuranosidase of family 54 glycoside hydrolase shows expanded substrate specificity
title_full	A novel fungal metal-dependent α-l-arabinofuranosidase of family 54 glycoside hydrolase shows expanded substrate specificity
title_fullStr	A novel fungal metal-dependent α-l-arabinofuranosidase of family 54 glycoside hydrolase shows expanded substrate specificity
title_full_unstemmed	A novel fungal metal-dependent α-l-arabinofuranosidase of family 54 glycoside hydrolase shows expanded substrate specificity
title_sort	novel fungal metal-dependent α-l-arabinofuranosidase of family 54 glycoside hydrolase shows expanded substrate specificity
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/0bb66bb4d5704a35bd1e0cb8f436517a
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A novel fungal metal-dependent α-l-arabinofuranosidase of family 54 glycoside hydrolase shows expanded substrate specificity

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