Characterisation of a “green” lipase from Aspergillus niger immobilised on polyethersulfone membranes

Detalhes bibliográficos
Autor(a) principal: Souza, Fernanda Martins de
Data de Publicação: 2019
Outros Autores: Soares, Cleide Mara Faria, Lima, Alvaro Silva, Santana, Luciana Cristina Lins de Aquino
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Acta scientiarum. Technology (Online)
Texto Completo: http://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/44498
Resumo: In this work, a “green” Aspergillus niger lipase obtained from the solid-state fermentation of Hancornia speciosa (“mangaba”) seeds was efficiently immobilised on polyethersulfone membranes (PES) by physical adsorption (PES-ADS-lipase) and covalent bonding (PES-COV-lipase) (immobilisation yields of 92 and 81%, respectively). The free lipase showed an optimum pH close to neutrality, while the biocatalysts displaced the pH to the alkaline region (optimum pH 9.0 and 11.0 for PES-ADS-lipase and PES-COV-lipase, respectively). The optimum temperature of free lipase was 55°C; however, a higher thermal stability occurred at 37°C. The PES-ADS-lipase and PES-COV-lipase showed lower optimum temperatures (37 and 45°C, respectively) but higher thermal stabilities at 45 and 55°C, respectively. The lower thermal inactivation constant and higher half-life of PES-COV-lipase at 55°C confirmed the efficiency of covalent bonding in maintaining the thermal stability of the enzyme. The Michaelis–Menten constant (Km) and maximum rate of reaction (Vmax) were also determined, and the biocatalysts showed higher affinities to substrates (lower Km values) than free lipase. In this work, the biocatalysts showed good catalytic properties with future potential applications in hydrolysis reactions. The use of a “green” lipase obtained from agroindustrial residue makes this product economically attractive from an industrial point of view.
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spelling Characterisation of a “green” lipase from Aspergillus niger immobilised on polyethersulfone membranesagroindustrial residue; enzyme; catalysis; polymeric supports.agroindustrial residue; enzyme; catalysis; polymeric supports.In this work, a “green” Aspergillus niger lipase obtained from the solid-state fermentation of Hancornia speciosa (“mangaba”) seeds was efficiently immobilised on polyethersulfone membranes (PES) by physical adsorption (PES-ADS-lipase) and covalent bonding (PES-COV-lipase) (immobilisation yields of 92 and 81%, respectively). The free lipase showed an optimum pH close to neutrality, while the biocatalysts displaced the pH to the alkaline region (optimum pH 9.0 and 11.0 for PES-ADS-lipase and PES-COV-lipase, respectively). The optimum temperature of free lipase was 55°C; however, a higher thermal stability occurred at 37°C. The PES-ADS-lipase and PES-COV-lipase showed lower optimum temperatures (37 and 45°C, respectively) but higher thermal stabilities at 45 and 55°C, respectively. The lower thermal inactivation constant and higher half-life of PES-COV-lipase at 55°C confirmed the efficiency of covalent bonding in maintaining the thermal stability of the enzyme. The Michaelis–Menten constant (Km) and maximum rate of reaction (Vmax) were also determined, and the biocatalysts showed higher affinities to substrates (lower Km values) than free lipase. In this work, the biocatalysts showed good catalytic properties with future potential applications in hydrolysis reactions. The use of a “green” lipase obtained from agroindustrial residue makes this product economically attractive from an industrial point of view.Universidade Estadual De Maringá2019-11-29info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/4449810.4025/actascitechnol.v42i1.44498Acta Scientiarum. Technology; Vol 42 (2020): Publicação contínua; e44498Acta Scientiarum. Technology; v. 42 (2020): Publicação contínua; e444981806-25631807-8664reponame:Acta scientiarum. Technology (Online)instname:Universidade Estadual de Maringá (UEM)instacron:UEMenghttp://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/44498/751375149029Copyright (c) 2020 Acta Scientiarum. Technologyhttps://creativecommons.org/licenses/by/4.0info:eu-repo/semantics/openAccessSouza, Fernanda Martins deSoares, Cleide Mara FariaLima, Alvaro SilvaSantana, Luciana Cristina Lins de Aquino2020-05-05T15:19:27Zoai:periodicos.uem.br/ojs:article/44498Revistahttps://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/indexPUBhttps://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/oai||actatech@uem.br1807-86641806-2563opendoar:2020-05-05T15:19:27Acta scientiarum. Technology (Online) - Universidade Estadual de Maringá (UEM)false
dc.title.none.fl_str_mv Characterisation of a “green” lipase from Aspergillus niger immobilised on polyethersulfone membranes
title Characterisation of a “green” lipase from Aspergillus niger immobilised on polyethersulfone membranes
spellingShingle Characterisation of a “green” lipase from Aspergillus niger immobilised on polyethersulfone membranes
Souza, Fernanda Martins de
agroindustrial residue; enzyme; catalysis; polymeric supports.
agroindustrial residue; enzyme; catalysis; polymeric supports.
title_short Characterisation of a “green” lipase from Aspergillus niger immobilised on polyethersulfone membranes
title_full Characterisation of a “green” lipase from Aspergillus niger immobilised on polyethersulfone membranes
title_fullStr Characterisation of a “green” lipase from Aspergillus niger immobilised on polyethersulfone membranes
title_full_unstemmed Characterisation of a “green” lipase from Aspergillus niger immobilised on polyethersulfone membranes
title_sort Characterisation of a “green” lipase from Aspergillus niger immobilised on polyethersulfone membranes
author Souza, Fernanda Martins de
author_facet Souza, Fernanda Martins de
Soares, Cleide Mara Faria
Lima, Alvaro Silva
Santana, Luciana Cristina Lins de Aquino
author_role author
author2 Soares, Cleide Mara Faria
Lima, Alvaro Silva
Santana, Luciana Cristina Lins de Aquino
author2_role author
author
author
dc.contributor.author.fl_str_mv Souza, Fernanda Martins de
Soares, Cleide Mara Faria
Lima, Alvaro Silva
Santana, Luciana Cristina Lins de Aquino
dc.subject.por.fl_str_mv agroindustrial residue; enzyme; catalysis; polymeric supports.
agroindustrial residue; enzyme; catalysis; polymeric supports.
topic agroindustrial residue; enzyme; catalysis; polymeric supports.
agroindustrial residue; enzyme; catalysis; polymeric supports.
description In this work, a “green” Aspergillus niger lipase obtained from the solid-state fermentation of Hancornia speciosa (“mangaba”) seeds was efficiently immobilised on polyethersulfone membranes (PES) by physical adsorption (PES-ADS-lipase) and covalent bonding (PES-COV-lipase) (immobilisation yields of 92 and 81%, respectively). The free lipase showed an optimum pH close to neutrality, while the biocatalysts displaced the pH to the alkaline region (optimum pH 9.0 and 11.0 for PES-ADS-lipase and PES-COV-lipase, respectively). The optimum temperature of free lipase was 55°C; however, a higher thermal stability occurred at 37°C. The PES-ADS-lipase and PES-COV-lipase showed lower optimum temperatures (37 and 45°C, respectively) but higher thermal stabilities at 45 and 55°C, respectively. The lower thermal inactivation constant and higher half-life of PES-COV-lipase at 55°C confirmed the efficiency of covalent bonding in maintaining the thermal stability of the enzyme. The Michaelis–Menten constant (Km) and maximum rate of reaction (Vmax) were also determined, and the biocatalysts showed higher affinities to substrates (lower Km values) than free lipase. In this work, the biocatalysts showed good catalytic properties with future potential applications in hydrolysis reactions. The use of a “green” lipase obtained from agroindustrial residue makes this product economically attractive from an industrial point of view.
publishDate 2019
dc.date.none.fl_str_mv 2019-11-29
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/44498
10.4025/actascitechnol.v42i1.44498
url http://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/44498
identifier_str_mv 10.4025/actascitechnol.v42i1.44498
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv http://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/44498/751375149029
dc.rights.driver.fl_str_mv Copyright (c) 2020 Acta Scientiarum. Technology
https://creativecommons.org/licenses/by/4.0
info:eu-repo/semantics/openAccess
rights_invalid_str_mv Copyright (c) 2020 Acta Scientiarum. Technology
https://creativecommons.org/licenses/by/4.0
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Universidade Estadual De Maringá
publisher.none.fl_str_mv Universidade Estadual De Maringá
dc.source.none.fl_str_mv Acta Scientiarum. Technology; Vol 42 (2020): Publicação contínua; e44498
Acta Scientiarum. Technology; v. 42 (2020): Publicação contínua; e44498
1806-2563
1807-8664
reponame:Acta scientiarum. Technology (Online)
instname:Universidade Estadual de Maringá (UEM)
instacron:UEM
instname_str Universidade Estadual de Maringá (UEM)
instacron_str UEM
institution UEM
reponame_str Acta scientiarum. Technology (Online)
collection Acta scientiarum. Technology (Online)
repository.name.fl_str_mv Acta scientiarum. Technology (Online) - Universidade Estadual de Maringá (UEM)
repository.mail.fl_str_mv ||actatech@uem.br
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