Microbial lipase obtained from the fermentation of pumpkin seeds: immobilization potential of hydrophobic matrices
Autor(a) principal: | |
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Data de Publicação: | 2014 |
Outros Autores: | , , , , |
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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Acta scientiarum. Technology (Online) |
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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 |
_version_ |
1799315335017398272 |