Natural montmorillonite as support for the immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571

Detalhes bibliográficos
Autor(a) principal: Coghetto, Chaline C.
Data de Publicação: 2012
Outros Autores: Scherer, Robison P., Silva, Marceli F., Golunski, Simone, Pergher, Sibele Berenice Castellã, Oliveira, Débora de, Oliveira, J. Vladimir, Treichel, Helen
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UFRN
Texto Completo: https://repositorio.ufrn.br/jspui/handle/123456789/29187
Resumo: The objective of this study was to investigate the process of immobilization of inulinases using natural montmorillonite as inorganic support. The enzyme to buffer ratio of 3:10 and 10 min of immobilization led to the highest specific activity, 375.07 U/mg protein. The immobilized inulinase kept its activity after 1968 h under storage at low temperatures and after 456–1826 h at high temperatures. The pH value of 3.5 led to the highest specific activity. Km values of 1.46 and 0.38 mM, and vmax of 0.2487 and 0.2396 mol/L min, were obtained, respectively, for sucrose and inulin.
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spelling Coghetto, Chaline C.Scherer, Robison P.Silva, Marceli F.Golunski, SimonePergher, Sibele Berenice CastellãOliveira, Débora deOliveira, J. VladimirTreichel, Helen2020-06-09T01:47:09Z2020-06-09T01:47:09Z2012-10COGHETTO, Chaline C.; SCHERER, Robison P.; SILVA, Marceli F.; GOLUNSKI, Simone; PERGHER, Sibele Berenice Castellã; OLIVEIRA, Débora de; OLIVEIRA, J. Vladimir; TREICHEL, Helen. Natural montmorillonite as support for the immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571. Biocatalysis And Agricultural Biotechnology, [s. l.], v. 1, n. 4, p. 284-289, out. 2012. ISSN 1878-8181. DOI https://doi.org/10.1016/j.bcab.2012.06.005. Disponível em: https://www.sciencedirect.com/science/article/abs/pii/S1878818112001028. Acesso em: 08 jun. 2020.1878-8181https://repositorio.ufrn.br/jspui/handle/123456789/2918710.1016/j.bcab.2012.06.005ElsevierKluyveromyces marxianus NRRL Y-7571InulinaseInorganic supportImmobilizationNatural montmorillonite as support for the immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleThe objective of this study was to investigate the process of immobilization of inulinases using natural montmorillonite as inorganic support. The enzyme to buffer ratio of 3:10 and 10 min of immobilization led to the highest specific activity, 375.07 U/mg protein. The immobilized inulinase kept its activity after 1968 h under storage at low temperatures and after 456–1826 h at high temperatures. The pH value of 3.5 led to the highest specific activity. Km values of 1.46 and 0.38 mM, and vmax of 0.2487 and 0.2396 mol/L min, were obtained, respectively, for sucrose and inulin.engreponame:Repositório Institucional da UFRNinstname:Universidade Federal do Rio Grande do Norte (UFRN)instacron:UFRNinfo:eu-repo/semantics/openAccessCC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-8914https://repositorio.ufrn.br/bitstream/123456789/29187/2/license_rdf4d2950bda3d176f570a9f8b328dfbbefMD52LICENSElicense.txtlicense.txttext/plain; charset=utf-81484https://repositorio.ufrn.br/bitstream/123456789/29187/3/license.txte9597aa2854d128fd968be5edc8a28d9MD53TEXTNaturalMontmorilloniteSupportImmobilization_Pergher_2012.pdf.txtNaturalMontmorilloniteSupportImmobilization_Pergher_2012.pdf.txtExtracted texttext/plain36278https://repositorio.ufrn.br/bitstream/123456789/29187/4/NaturalMontmorilloniteSupportImmobilization_Pergher_2012.pdf.txt42966cc7a8c5daa37951cc1e288f91b2MD54THUMBNAILNaturalMontmorilloniteSupportImmobilization_Pergher_2012.pdf.jpgNaturalMontmorilloniteSupportImmobilization_Pergher_2012.pdf.jpgGenerated Thumbnailimage/jpeg1755https://repositorio.ufrn.br/bitstream/123456789/29187/5/NaturalMontmorilloniteSupportImmobilization_Pergher_2012.pdf.jpg5bf7a6313c0c0f2bb73cd7ba8a598012MD55123456789/291872023-01-26 14:54:54.116oai:https://repositorio.ufrn.br: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Repositório de PublicaçõesPUBhttp://repositorio.ufrn.br/oai/opendoar:2023-01-26T17:54:54Repositório Institucional da UFRN - Universidade Federal do Rio Grande do Norte (UFRN)false
dc.title.pt_BR.fl_str_mv Natural montmorillonite as support for the immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571
title Natural montmorillonite as support for the immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571
spellingShingle Natural montmorillonite as support for the immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571
Coghetto, Chaline C.
Kluyveromyces marxianus NRRL Y-7571
Inulinase
Inorganic support
Immobilization
title_short Natural montmorillonite as support for the immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571
title_full Natural montmorillonite as support for the immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571
title_fullStr Natural montmorillonite as support for the immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571
title_full_unstemmed Natural montmorillonite as support for the immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571
title_sort Natural montmorillonite as support for the immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571
author Coghetto, Chaline C.
author_facet Coghetto, Chaline C.
Scherer, Robison P.
Silva, Marceli F.
Golunski, Simone
Pergher, Sibele Berenice Castellã
Oliveira, Débora de
Oliveira, J. Vladimir
Treichel, Helen
author_role author
author2 Scherer, Robison P.
Silva, Marceli F.
Golunski, Simone
Pergher, Sibele Berenice Castellã
Oliveira, Débora de
Oliveira, J. Vladimir
Treichel, Helen
author2_role author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Coghetto, Chaline C.
Scherer, Robison P.
Silva, Marceli F.
Golunski, Simone
Pergher, Sibele Berenice Castellã
Oliveira, Débora de
Oliveira, J. Vladimir
Treichel, Helen
dc.subject.por.fl_str_mv Kluyveromyces marxianus NRRL Y-7571
Inulinase
Inorganic support
Immobilization
topic Kluyveromyces marxianus NRRL Y-7571
Inulinase
Inorganic support
Immobilization
description The objective of this study was to investigate the process of immobilization of inulinases using natural montmorillonite as inorganic support. The enzyme to buffer ratio of 3:10 and 10 min of immobilization led to the highest specific activity, 375.07 U/mg protein. The immobilized inulinase kept its activity after 1968 h under storage at low temperatures and after 456–1826 h at high temperatures. The pH value of 3.5 led to the highest specific activity. Km values of 1.46 and 0.38 mM, and vmax of 0.2487 and 0.2396 mol/L min, were obtained, respectively, for sucrose and inulin.
publishDate 2012
dc.date.issued.fl_str_mv 2012-10
dc.date.accessioned.fl_str_mv 2020-06-09T01:47:09Z
dc.date.available.fl_str_mv 2020-06-09T01:47:09Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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dc.identifier.citation.fl_str_mv COGHETTO, Chaline C.; SCHERER, Robison P.; SILVA, Marceli F.; GOLUNSKI, Simone; PERGHER, Sibele Berenice Castellã; OLIVEIRA, Débora de; OLIVEIRA, J. Vladimir; TREICHEL, Helen. Natural montmorillonite as support for the immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571. Biocatalysis And Agricultural Biotechnology, [s. l.], v. 1, n. 4, p. 284-289, out. 2012. ISSN 1878-8181. DOI https://doi.org/10.1016/j.bcab.2012.06.005. Disponível em: https://www.sciencedirect.com/science/article/abs/pii/S1878818112001028. Acesso em: 08 jun. 2020.
dc.identifier.uri.fl_str_mv https://repositorio.ufrn.br/jspui/handle/123456789/29187
dc.identifier.issn.none.fl_str_mv 1878-8181
dc.identifier.doi.none.fl_str_mv 10.1016/j.bcab.2012.06.005
identifier_str_mv COGHETTO, Chaline C.; SCHERER, Robison P.; SILVA, Marceli F.; GOLUNSKI, Simone; PERGHER, Sibele Berenice Castellã; OLIVEIRA, Débora de; OLIVEIRA, J. Vladimir; TREICHEL, Helen. Natural montmorillonite as support for the immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571. Biocatalysis And Agricultural Biotechnology, [s. l.], v. 1, n. 4, p. 284-289, out. 2012. ISSN 1878-8181. DOI https://doi.org/10.1016/j.bcab.2012.06.005. Disponível em: https://www.sciencedirect.com/science/article/abs/pii/S1878818112001028. Acesso em: 08 jun. 2020.
1878-8181
10.1016/j.bcab.2012.06.005
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