Salt-tolerant α-arabinofuranosidase from a new specie Aspergillus hortai CRM1919: Production in acid conditions, purification, characterization and application on xylan hydrolysis
Autor(a) principal: | |
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Data de Publicação: | 2020 |
Outros Autores: | , , , |
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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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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1808128630483582976 |