Salt-tolerant α-arabinofuranosidase from a new specie Aspergillus hortai CRM1919: Production in acid conditions, purification, characterization and application on xylan hydrolysis

Detalhes bibliográficos
Autor(a) principal: Terrone, Cárol Cabral [UNESP]
Data de Publicação: 2020
Outros Autores: Montesino de Freitas Nascimento, Juliana [UNESP], Fanchini Terrasan, César Rafael, Brienzo, Michel [UNESP], Carmona, Eleonora Cano [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1016/j.bcab.2019.101460
http://hdl.handle.net/11449/199819
Resumo: Hemicelluloses are mainly branched heteropolysaccharides composed by xylose, arabinose, mannose, galactose, rhamnose and glucose. The main hemicellulose is xylan, a structure composed by xylose main chain branched with other monosaccharides or glucuronic and galacturonic acids. Among various hydrolytic enzymes acting on the degradation of xylan, α-L-arabinofuranosidases catalyze the hydrolysis of linkages between α-L-arabinofuranosides and the polysaccharide main chain. In this study, Aspergillus hortai strain CRM1919, isolated from soil surrounding saline and alkaline lagoons of the Nhecolândia region in Pantanal Matogrossense was investigated regarding the production of α-L-arabinofuranosidases. A. hortai produced α-L-arabinofuranosidase at high levels when cultivated in medium containing citrus pulp and orange peel at 1% (w/v) under static submerged cultures for 4 days and at pH 2.5 and 30 °C. The optimization steps increased 15-fold the enzymatic activity. The purified α-L-arabinofuranosidase was optimally active at pH of 4.0 and 60 °C, presenting half-lives of 265 and 230 min at 30 and 40 °C, respectively. High enzyme stability was observed after 24 h incubation at pH 5.0 and in presence of high concentration of NaCl in the reaction medium. The purified enzyme was mainly active against ρ-nitrophenyl-α-L-arabinofuranoside presenting the following kinetic parameters Km of 8.73 mmol/L, Vmax of 7.91 μmol/min.mg of protein and Kcat of 0.59/min. Hydrolysis of oat xylan performed in the presence of the purified α-arabinofuranosidase individually and in association with a purified xylanase made possible to verify the cooperation between these xylanolytic enzymes and the sequential action of each enzyme in the xylan structure hydrolysis.
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spelling Salt-tolerant α-arabinofuranosidase from a new specie Aspergillus hortai CRM1919: Production in acid conditions, purification, characterization and application on xylan hydrolysisAccessory enzymesCitrus pulpEnzymes cooperationGlycoside hydrolasesxylan‐degrading enzymesα-L-arabinofuranosidaseHemicelluloses are mainly branched heteropolysaccharides composed by xylose, arabinose, mannose, galactose, rhamnose and glucose. The main hemicellulose is xylan, a structure composed by xylose main chain branched with other monosaccharides or glucuronic and galacturonic acids. Among various hydrolytic enzymes acting on the degradation of xylan, α-L-arabinofuranosidases catalyze the hydrolysis of linkages between α-L-arabinofuranosides and the polysaccharide main chain. In this study, Aspergillus hortai strain CRM1919, isolated from soil surrounding saline and alkaline lagoons of the Nhecolândia region in Pantanal Matogrossense was investigated regarding the production of α-L-arabinofuranosidases. A. hortai produced α-L-arabinofuranosidase at high levels when cultivated in medium containing citrus pulp and orange peel at 1% (w/v) under static submerged cultures for 4 days and at pH 2.5 and 30 °C. The optimization steps increased 15-fold the enzymatic activity. The purified α-L-arabinofuranosidase was optimally active at pH of 4.0 and 60 °C, presenting half-lives of 265 and 230 min at 30 and 40 °C, respectively. High enzyme stability was observed after 24 h incubation at pH 5.0 and in presence of high concentration of NaCl in the reaction medium. The purified enzyme was mainly active against ρ-nitrophenyl-α-L-arabinofuranoside presenting the following kinetic parameters Km of 8.73 mmol/L, Vmax of 7.91 μmol/min.mg of protein and Kcat of 0.59/min. Hydrolysis of oat xylan performed in the presence of the purified α-arabinofuranosidase individually and in association with a purified xylanase made possible to verify the cooperation between these xylanolytic enzymes and the sequential action of each enzyme in the xylan structure hydrolysis.Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Bioenergy Research Institute Univ Estadual Paulista - UNESP, São PauloBiochemistry and Microbiology Department Bioscience Institute Univ Estadual Paulista - UNESP, São PauloDepartment of Biochemistry and Tissue Biology Institute of Biology Univ Campinas – UNICAMP, São PauloBioenergy Research Institute Univ Estadual Paulista - UNESP, São PauloBiochemistry and Microbiology Department Bioscience Institute Univ Estadual Paulista - UNESP, São PauloUniversidade Estadual Paulista (Unesp)Universidade Estadual de Campinas (UNICAMP)Terrone, Cárol Cabral [UNESP]Montesino de Freitas Nascimento, Juliana [UNESP]Fanchini Terrasan, César RafaelBrienzo, Michel [UNESP]Carmona, Eleonora Cano [UNESP]2020-12-12T01:50:11Z2020-12-12T01:50:11Z2020-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1016/j.bcab.2019.101460Biocatalysis and Agricultural Biotechnology, v. 23.1878-8181http://hdl.handle.net/11449/19981910.1016/j.bcab.2019.1014602-s2.0-850765602198251885707409794Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBiocatalysis and Agricultural Biotechnologyinfo:eu-repo/semantics/openAccess2021-10-23T10:02:13Zoai:repositorio.unesp.br:11449/199819Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T16:17:46.688521Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Salt-tolerant α-arabinofuranosidase from a new specie Aspergillus hortai CRM1919: Production in acid conditions, purification, characterization and application on xylan hydrolysis
title Salt-tolerant α-arabinofuranosidase from a new specie Aspergillus hortai CRM1919: Production in acid conditions, purification, characterization and application on xylan hydrolysis
spellingShingle Salt-tolerant α-arabinofuranosidase from a new specie Aspergillus hortai CRM1919: Production in acid conditions, purification, characterization and application on xylan hydrolysis
Terrone, Cárol Cabral [UNESP]
Accessory enzymes
Citrus pulp
Enzymes cooperation
Glycoside hydrolases
xylan‐degrading enzymes
α-L-arabinofuranosidase
title_short Salt-tolerant α-arabinofuranosidase from a new specie Aspergillus hortai CRM1919: Production in acid conditions, purification, characterization and application on xylan hydrolysis
title_full Salt-tolerant α-arabinofuranosidase from a new specie Aspergillus hortai CRM1919: Production in acid conditions, purification, characterization and application on xylan hydrolysis
title_fullStr Salt-tolerant α-arabinofuranosidase from a new specie Aspergillus hortai CRM1919: Production in acid conditions, purification, characterization and application on xylan hydrolysis
title_full_unstemmed Salt-tolerant α-arabinofuranosidase from a new specie Aspergillus hortai CRM1919: Production in acid conditions, purification, characterization and application on xylan hydrolysis
title_sort Salt-tolerant α-arabinofuranosidase from a new specie Aspergillus hortai CRM1919: Production in acid conditions, purification, characterization and application on xylan hydrolysis
author Terrone, Cárol Cabral [UNESP]
author_facet Terrone, Cárol Cabral [UNESP]
Montesino de Freitas Nascimento, Juliana [UNESP]
Fanchini Terrasan, César Rafael
Brienzo, Michel [UNESP]
Carmona, Eleonora Cano [UNESP]
author_role author
author2 Montesino de Freitas Nascimento, Juliana [UNESP]
Fanchini Terrasan, César Rafael
Brienzo, Michel [UNESP]
Carmona, Eleonora Cano [UNESP]
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
Universidade Estadual de Campinas (UNICAMP)
dc.contributor.author.fl_str_mv Terrone, Cárol Cabral [UNESP]
Montesino de Freitas Nascimento, Juliana [UNESP]
Fanchini Terrasan, César Rafael
Brienzo, Michel [UNESP]
Carmona, Eleonora Cano [UNESP]
dc.subject.por.fl_str_mv Accessory enzymes
Citrus pulp
Enzymes cooperation
Glycoside hydrolases
xylan‐degrading enzymes
α-L-arabinofuranosidase
topic Accessory enzymes
Citrus pulp
Enzymes cooperation
Glycoside hydrolases
xylan‐degrading enzymes
α-L-arabinofuranosidase
description Hemicelluloses are mainly branched heteropolysaccharides composed by xylose, arabinose, mannose, galactose, rhamnose and glucose. The main hemicellulose is xylan, a structure composed by xylose main chain branched with other monosaccharides or glucuronic and galacturonic acids. Among various hydrolytic enzymes acting on the degradation of xylan, α-L-arabinofuranosidases catalyze the hydrolysis of linkages between α-L-arabinofuranosides and the polysaccharide main chain. In this study, Aspergillus hortai strain CRM1919, isolated from soil surrounding saline and alkaline lagoons of the Nhecolândia region in Pantanal Matogrossense was investigated regarding the production of α-L-arabinofuranosidases. A. hortai produced α-L-arabinofuranosidase at high levels when cultivated in medium containing citrus pulp and orange peel at 1% (w/v) under static submerged cultures for 4 days and at pH 2.5 and 30 °C. The optimization steps increased 15-fold the enzymatic activity. The purified α-L-arabinofuranosidase was optimally active at pH of 4.0 and 60 °C, presenting half-lives of 265 and 230 min at 30 and 40 °C, respectively. High enzyme stability was observed after 24 h incubation at pH 5.0 and in presence of high concentration of NaCl in the reaction medium. The purified enzyme was mainly active against ρ-nitrophenyl-α-L-arabinofuranoside presenting the following kinetic parameters Km of 8.73 mmol/L, Vmax of 7.91 μmol/min.mg of protein and Kcat of 0.59/min. Hydrolysis of oat xylan performed in the presence of the purified α-arabinofuranosidase individually and in association with a purified xylanase made possible to verify the cooperation between these xylanolytic enzymes and the sequential action of each enzyme in the xylan structure hydrolysis.
publishDate 2020
dc.date.none.fl_str_mv 2020-12-12T01:50:11Z
2020-12-12T01:50:11Z
2020-01-01
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1016/j.bcab.2019.101460
Biocatalysis and Agricultural Biotechnology, v. 23.
1878-8181
http://hdl.handle.net/11449/199819
10.1016/j.bcab.2019.101460
2-s2.0-85076560219
8251885707409794
url http://dx.doi.org/10.1016/j.bcab.2019.101460
http://hdl.handle.net/11449/199819
identifier_str_mv Biocatalysis and Agricultural Biotechnology, v. 23.
1878-8181
10.1016/j.bcab.2019.101460
2-s2.0-85076560219
8251885707409794
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Biocatalysis and Agricultural Biotechnology
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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