Partial characterization of an inulinase produced by Aspergillus japonicus URM5633
Autor(a) principal: | |
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Data de Publicação: | 2012 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Archives of Biology and Technology |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132012000500005 |
Resumo: | Enzymes obtained by fermentation processes offer a number of advantages and have been widely researched and used throughout the world. This study aimed to partially characterise an inulinase produced from palm and cassava peel. The enzyme was produced via the solid-state fermentation of Aspergillus japonicus URM5633. The optimal temperatures were 50ºC and 55ºC, and the optimal pH values were 5.2 and 3.4 for inulinase fermentatively produced from palm and cassava peel, respectively. The thermostability measurements for inulinase produced in palm showed that the relative activity remained below 100% until 30 minutes of stability for all temperatures, but reached 106.8% at a temperature of 50ºC after 60 minutes. Inulinase from the crude extract of cassava peel was pH stable and only decreased to 55% of the maximal activity over the course of the assay, suggesting that this enzyme can be used in inulinase production and can be utilized in food industries. |
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Brazilian Archives of Biology and Technology |
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Partial characterization of an inulinase produced by Aspergillus japonicus URM5633inulinasecharacterisationsolid-state fermentationAspergillus japonicusEnzymes obtained by fermentation processes offer a number of advantages and have been widely researched and used throughout the world. This study aimed to partially characterise an inulinase produced from palm and cassava peel. The enzyme was produced via the solid-state fermentation of Aspergillus japonicus URM5633. The optimal temperatures were 50ºC and 55ºC, and the optimal pH values were 5.2 and 3.4 for inulinase fermentatively produced from palm and cassava peel, respectively. The thermostability measurements for inulinase produced in palm showed that the relative activity remained below 100% until 30 minutes of stability for all temperatures, but reached 106.8% at a temperature of 50ºC after 60 minutes. Inulinase from the crude extract of cassava peel was pH stable and only decreased to 55% of the maximal activity over the course of the assay, suggesting that this enzyme can be used in inulinase production and can be utilized in food industries.Instituto de Tecnologia do Paraná - Tecpar2012-10-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132012000500005Brazilian Archives of Biology and Technology v.55 n.5 2012reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/S1516-89132012000500005info:eu-repo/semantics/openAccessSilva,Anna Carolina daQueiroz,Alana Emilia Soares de FrançaPorto,Tatiana SouzaSpier,Michele RigonSoccol,Carlos RicardoPorto,Ana Lúcia FigueiredoSouza-Motta,Cristina MariaMoreira,Keila Aparecidaeng2012-10-09T00:00:00Zoai:scielo:S1516-89132012000500005Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2012-10-09T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false |
dc.title.none.fl_str_mv |
Partial characterization of an inulinase produced by Aspergillus japonicus URM5633 |
title |
Partial characterization of an inulinase produced by Aspergillus japonicus URM5633 |
spellingShingle |
Partial characterization of an inulinase produced by Aspergillus japonicus URM5633 Silva,Anna Carolina da inulinase characterisation solid-state fermentation Aspergillus japonicus |
title_short |
Partial characterization of an inulinase produced by Aspergillus japonicus URM5633 |
title_full |
Partial characterization of an inulinase produced by Aspergillus japonicus URM5633 |
title_fullStr |
Partial characterization of an inulinase produced by Aspergillus japonicus URM5633 |
title_full_unstemmed |
Partial characterization of an inulinase produced by Aspergillus japonicus URM5633 |
title_sort |
Partial characterization of an inulinase produced by Aspergillus japonicus URM5633 |
author |
Silva,Anna Carolina da |
author_facet |
Silva,Anna Carolina da Queiroz,Alana Emilia Soares de França Porto,Tatiana Souza Spier,Michele Rigon Soccol,Carlos Ricardo Porto,Ana Lúcia Figueiredo Souza-Motta,Cristina Maria Moreira,Keila Aparecida |
author_role |
author |
author2 |
Queiroz,Alana Emilia Soares de França Porto,Tatiana Souza Spier,Michele Rigon Soccol,Carlos Ricardo Porto,Ana Lúcia Figueiredo Souza-Motta,Cristina Maria Moreira,Keila Aparecida |
author2_role |
author author author author author author author |
dc.contributor.author.fl_str_mv |
Silva,Anna Carolina da Queiroz,Alana Emilia Soares de França Porto,Tatiana Souza Spier,Michele Rigon Soccol,Carlos Ricardo Porto,Ana Lúcia Figueiredo Souza-Motta,Cristina Maria Moreira,Keila Aparecida |
dc.subject.por.fl_str_mv |
inulinase characterisation solid-state fermentation Aspergillus japonicus |
topic |
inulinase characterisation solid-state fermentation Aspergillus japonicus |
description |
Enzymes obtained by fermentation processes offer a number of advantages and have been widely researched and used throughout the world. This study aimed to partially characterise an inulinase produced from palm and cassava peel. The enzyme was produced via the solid-state fermentation of Aspergillus japonicus URM5633. The optimal temperatures were 50ºC and 55ºC, and the optimal pH values were 5.2 and 3.4 for inulinase fermentatively produced from palm and cassava peel, respectively. The thermostability measurements for inulinase produced in palm showed that the relative activity remained below 100% until 30 minutes of stability for all temperatures, but reached 106.8% at a temperature of 50ºC after 60 minutes. Inulinase from the crude extract of cassava peel was pH stable and only decreased to 55% of the maximal activity over the course of the assay, suggesting that this enzyme can be used in inulinase production and can be utilized in food industries. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-10-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132012000500005 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132012000500005 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1516-89132012000500005 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Instituto de Tecnologia do Paraná - Tecpar |
publisher.none.fl_str_mv |
Instituto de Tecnologia do Paraná - Tecpar |
dc.source.none.fl_str_mv |
Brazilian Archives of Biology and Technology v.55 n.5 2012 reponame:Brazilian Archives of Biology and Technology instname:Instituto de Tecnologia do Paraná (Tecpar) instacron:TECPAR |
instname_str |
Instituto de Tecnologia do Paraná (Tecpar) |
instacron_str |
TECPAR |
institution |
TECPAR |
reponame_str |
Brazilian Archives of Biology and Technology |
collection |
Brazilian Archives of Biology and Technology |
repository.name.fl_str_mv |
Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar) |
repository.mail.fl_str_mv |
babt@tecpar.br||babt@tecpar.br |
_version_ |
1750318275263201280 |