Microbial lipase obtained from the fermentation of pumpkin seeds: immobilization potential of hydrophobic matrices

Detalhes bibliográficos
Autor(a) principal: Santos, Rafaela Cristiane Andrade
Data de Publicação: 2014
Outros Autores: Araújo, Kyzzes Barreto, Zubiolo, Claúdia, Soares, Cleide Mara Faria, Lima, Alvaro Silva, Aquino, Luciana Cristina Lins de Santana
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/18275
Resumo: Immobilization potential of lipase from Aspergillus niger on sol-gel matrix was evaluated by physical adsorption and covalent binding and the biochemical characterization of free and immobilized enzyme was performed. Lipase was produced by solid state fermentation of pumpkin seed flour with 30% moisture, at 30°C for 120h. The enzyme was pre-purified with ammonium sulfate and immobilized in the sol-gel matrix by covalent attachment and physical adsorption. A higher yield of immobilization (81.88%) was obtained in the latter. The free enzyme presented higher hydrolytic activity with pH 4.0, at 37°C; moreover, it was more stable with pH between 6.0 and 7.0, at 35°C. The immobilized lipase showed maximum hydrolytic activity with pH 11.0, at 50°C; it was more stable with pH 11.0, at 37°C. Parameters Km and Vmax were best determined by Hanes-Woolf linearization. 
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spelling Microbial lipase obtained from the fermentation of pumpkin seeds: immobilization potential of hydrophobic matricesenzymesol-gelagroindustrial residueciencias agráriasImmobilization potential of lipase from Aspergillus niger on sol-gel matrix was evaluated by physical adsorption and covalent binding and the biochemical characterization of free and immobilized enzyme was performed. Lipase was produced by solid state fermentation of pumpkin seed flour with 30% moisture, at 30°C for 120h. The enzyme was pre-purified with ammonium sulfate and immobilized in the sol-gel matrix by covalent attachment and physical adsorption. A higher yield of immobilization (81.88%) was obtained in the latter. The free enzyme presented higher hydrolytic activity with pH 4.0, at 37°C; moreover, it was more stable with pH between 6.0 and 7.0, at 35°C. The immobilized lipase showed maximum hydrolytic activity with pH 11.0, at 50°C; it was more stable with pH 11.0, at 37°C. Parameters Km and Vmax were best determined by Hanes-Woolf linearization. Universidade Estadual De Maringá2014-04-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/1827510.4025/actascitechnol.v36i2.18275Acta Scientiarum. Technology; Vol 36 No 2 (2014); 193-201Acta Scientiarum. Technology; v. 36 n. 2 (2014); 193-2011806-25631807-8664reponame:Acta scientiarum. Technology (Online)instname:Universidade Estadual de Maringá (UEM)instacron:UEMenghttp://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/18275/12644Santos, Rafaela Cristiane AndradeAraújo, Kyzzes BarretoZubiolo, ClaúdiaSoares, Cleide Mara FariaLima, Alvaro SilvaAquino, Luciana Cristina Lins de Santanainfo:eu-repo/semantics/openAccess2014-04-04T15:34:15Zoai:periodicos.uem.br/ojs:article/18275Revistahttps://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/indexPUBhttps://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/oai||actatech@uem.br1807-86641806-2563opendoar:2014-04-04T15:34:15Acta scientiarum. Technology (Online) - Universidade Estadual de Maringá (UEM)false
dc.title.none.fl_str_mv Microbial lipase obtained from the fermentation of pumpkin seeds: immobilization potential of hydrophobic matrices
title Microbial lipase obtained from the fermentation of pumpkin seeds: immobilization potential of hydrophobic matrices
spellingShingle Microbial lipase obtained from the fermentation of pumpkin seeds: immobilization potential of hydrophobic matrices
Santos, Rafaela Cristiane Andrade
enzyme
sol-gel
agroindustrial residue
ciencias agrárias
title_short Microbial lipase obtained from the fermentation of pumpkin seeds: immobilization potential of hydrophobic matrices
title_full Microbial lipase obtained from the fermentation of pumpkin seeds: immobilization potential of hydrophobic matrices
title_fullStr Microbial lipase obtained from the fermentation of pumpkin seeds: immobilization potential of hydrophobic matrices
title_full_unstemmed Microbial lipase obtained from the fermentation of pumpkin seeds: immobilization potential of hydrophobic matrices
title_sort Microbial lipase obtained from the fermentation of pumpkin seeds: immobilization potential of hydrophobic matrices
author Santos, Rafaela Cristiane Andrade
author_facet Santos, Rafaela Cristiane Andrade
Araújo, Kyzzes Barreto
Zubiolo, Claúdia
Soares, Cleide Mara Faria
Lima, Alvaro Silva
Aquino, Luciana Cristina Lins de Santana
author_role author
author2 Araújo, Kyzzes Barreto
Zubiolo, Claúdia
Soares, Cleide Mara Faria
Lima, Alvaro Silva
Aquino, Luciana Cristina Lins de Santana
author2_role author
author
author
author
author
dc.contributor.author.fl_str_mv Santos, Rafaela Cristiane Andrade
Araújo, Kyzzes Barreto
Zubiolo, Claúdia
Soares, Cleide Mara Faria
Lima, Alvaro Silva
Aquino, Luciana Cristina Lins de Santana
dc.subject.por.fl_str_mv enzyme
sol-gel
agroindustrial residue
ciencias agrárias
topic enzyme
sol-gel
agroindustrial residue
ciencias agrárias
description Immobilization potential of lipase from Aspergillus niger on sol-gel matrix was evaluated by physical adsorption and covalent binding and the biochemical characterization of free and immobilized enzyme was performed. Lipase was produced by solid state fermentation of pumpkin seed flour with 30% moisture, at 30°C for 120h. The enzyme was pre-purified with ammonium sulfate and immobilized in the sol-gel matrix by covalent attachment and physical adsorption. A higher yield of immobilization (81.88%) was obtained in the latter. The free enzyme presented higher hydrolytic activity with pH 4.0, at 37°C; moreover, it was more stable with pH between 6.0 and 7.0, at 35°C. The immobilized lipase showed maximum hydrolytic activity with pH 11.0, at 50°C; it was more stable with pH 11.0, at 37°C. Parameters Km and Vmax were best determined by Hanes-Woolf linearization. 
publishDate 2014
dc.date.none.fl_str_mv 2014-04-04
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/18275
10.4025/actascitechnol.v36i2.18275
url http://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/18275
identifier_str_mv 10.4025/actascitechnol.v36i2.18275
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/18275/12644
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
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 36 No 2 (2014); 193-201
Acta Scientiarum. Technology; v. 36 n. 2 (2014); 193-201
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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