Characterization of an exoinulinase produced by Aspergillus terreus CCT 4083 grown on sugar cane bagasse

Detalhes bibliográficos
Autor(a) principal: Coitinho, Juliana B.
Data de Publicação: 2010
Outros Autores: Guimarães, Valéria M., Almeida, Maíra N. de, Falkoski, Daniel L., Queiróz, José H. de, Rezende, Sebastião T. de
Tipo de documento: Artigo
Idioma: eng
Título da fonte: LOCUS Repositório Institucional da UFV
Texto Completo: https://doi.org/10.1021/jf1011159
http://www.locus.ufv.br/handle/123456789/19436
Resumo: Exoinulinase (β- D -fructan fructohydrolase, EC 3.2.1.80) secreted by Aspergillus terreus CCT4083 was obtained using sugar cane bagasse, an agroindustrial residue, as a carbon source. It was further purified from the supernatant culture in a rapid procedure. The enzyme presented 57 kDa on SDS-PAGE and 56 kDa on gel filtration chromatography. Inulin was hydrolyzed by the purified enzyme, yielding D -fructose as the main product. This enzyme showed maximum activity at pH 4.0 and 60 °C and maintained more than 90 and 75% of its original activity at 40 and 50 °C, respectively, after 3.5 h of preincubation. The K M values for inulin, sucrose, and raffinose were 11, 4.20, and 27.89 mM, respectively, and D -fructose was a competitive inhibitor (K i = 47.55 mM). The activation energies for sucrose, raffinose, and inulin were 10.4, 5.61, and 4.44 kcal/mol, respectively. The characteristics of A. terreus exoinulinase were compared to those of inulinases isolated from other organisms. The exoinulinase traits presented especially good thermostability and the ability to produce pure D -fructose, suggesting its application to the production of high-fructose syrup.
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spelling Coitinho, Juliana B.Guimarães, Valéria M.Almeida, Maíra N. deFalkoski, Daniel L.Queiróz, José H. deRezende, Sebastião T. de2018-05-10T12:08:58Z2018-05-10T12:08:58Z2010-02-0715205118https://doi.org/10.1021/jf1011159http://www.locus.ufv.br/handle/123456789/19436Exoinulinase (β- D -fructan fructohydrolase, EC 3.2.1.80) secreted by Aspergillus terreus CCT4083 was obtained using sugar cane bagasse, an agroindustrial residue, as a carbon source. It was further purified from the supernatant culture in a rapid procedure. The enzyme presented 57 kDa on SDS-PAGE and 56 kDa on gel filtration chromatography. Inulin was hydrolyzed by the purified enzyme, yielding D -fructose as the main product. This enzyme showed maximum activity at pH 4.0 and 60 °C and maintained more than 90 and 75% of its original activity at 40 and 50 °C, respectively, after 3.5 h of preincubation. The K M values for inulin, sucrose, and raffinose were 11, 4.20, and 27.89 mM, respectively, and D -fructose was a competitive inhibitor (K i = 47.55 mM). The activation energies for sucrose, raffinose, and inulin were 10.4, 5.61, and 4.44 kcal/mol, respectively. The characteristics of A. terreus exoinulinase were compared to those of inulinases isolated from other organisms. The exoinulinase traits presented especially good thermostability and the ability to produce pure D -fructose, suggesting its application to the production of high-fructose syrup.engJournal of Agricultural and Food Chemistryv. 58, n. 14, p. 8386–8391, July 2010American Chemical Societyinfo:eu-repo/semantics/openAccessInulinaseAspergillus terreus CCT4083inulinAgroindustrial residueCharacterization of an exoinulinase produced by Aspergillus terreus CCT 4083 grown on sugar cane bagasseinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFVORIGINALartigo.pdfartigo.pdfTexto completoapplication/pdf2757531https://locus.ufv.br//bitstream/123456789/19436/1/artigo.pdfaf32009856873632353663c934711892MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://locus.ufv.br//bitstream/123456789/19436/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52THUMBNAILartigo.pdf.jpgartigo.pdf.jpgIM Thumbnailimage/jpeg6258https://locus.ufv.br//bitstream/123456789/19436/3/artigo.pdf.jpg3c5472a06cc9c9b9257f5cce7668eec8MD53123456789/194362018-05-10 23:00:55.163oai:locus.ufv.br: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Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452018-05-11T02:00:55LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false
dc.title.en.fl_str_mv Characterization of an exoinulinase produced by Aspergillus terreus CCT 4083 grown on sugar cane bagasse
title Characterization of an exoinulinase produced by Aspergillus terreus CCT 4083 grown on sugar cane bagasse
spellingShingle Characterization of an exoinulinase produced by Aspergillus terreus CCT 4083 grown on sugar cane bagasse
Coitinho, Juliana B.
Inulinase
Aspergillus terreus CCT4083
inulin
Agroindustrial residue
title_short Characterization of an exoinulinase produced by Aspergillus terreus CCT 4083 grown on sugar cane bagasse
title_full Characterization of an exoinulinase produced by Aspergillus terreus CCT 4083 grown on sugar cane bagasse
title_fullStr Characterization of an exoinulinase produced by Aspergillus terreus CCT 4083 grown on sugar cane bagasse
title_full_unstemmed Characterization of an exoinulinase produced by Aspergillus terreus CCT 4083 grown on sugar cane bagasse
title_sort Characterization of an exoinulinase produced by Aspergillus terreus CCT 4083 grown on sugar cane bagasse
author Coitinho, Juliana B.
author_facet Coitinho, Juliana B.
Guimarães, Valéria M.
Almeida, Maíra N. de
Falkoski, Daniel L.
Queiróz, José H. de
Rezende, Sebastião T. de
author_role author
author2 Guimarães, Valéria M.
Almeida, Maíra N. de
Falkoski, Daniel L.
Queiróz, José H. de
Rezende, Sebastião T. de
author2_role author
author
author
author
author
dc.contributor.author.fl_str_mv Coitinho, Juliana B.
Guimarães, Valéria M.
Almeida, Maíra N. de
Falkoski, Daniel L.
Queiróz, José H. de
Rezende, Sebastião T. de
dc.subject.pt-BR.fl_str_mv Inulinase
Aspergillus terreus CCT4083
inulin
Agroindustrial residue
topic Inulinase
Aspergillus terreus CCT4083
inulin
Agroindustrial residue
description Exoinulinase (β- D -fructan fructohydrolase, EC 3.2.1.80) secreted by Aspergillus terreus CCT4083 was obtained using sugar cane bagasse, an agroindustrial residue, as a carbon source. It was further purified from the supernatant culture in a rapid procedure. The enzyme presented 57 kDa on SDS-PAGE and 56 kDa on gel filtration chromatography. Inulin was hydrolyzed by the purified enzyme, yielding D -fructose as the main product. This enzyme showed maximum activity at pH 4.0 and 60 °C and maintained more than 90 and 75% of its original activity at 40 and 50 °C, respectively, after 3.5 h of preincubation. The K M values for inulin, sucrose, and raffinose were 11, 4.20, and 27.89 mM, respectively, and D -fructose was a competitive inhibitor (K i = 47.55 mM). The activation energies for sucrose, raffinose, and inulin were 10.4, 5.61, and 4.44 kcal/mol, respectively. The characteristics of A. terreus exoinulinase were compared to those of inulinases isolated from other organisms. The exoinulinase traits presented especially good thermostability and the ability to produce pure D -fructose, suggesting its application to the production of high-fructose syrup.
publishDate 2010
dc.date.issued.fl_str_mv 2010-02-07
dc.date.accessioned.fl_str_mv 2018-05-10T12:08:58Z
dc.date.available.fl_str_mv 2018-05-10T12:08:58Z
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.uri.fl_str_mv https://doi.org/10.1021/jf1011159
http://www.locus.ufv.br/handle/123456789/19436
dc.identifier.issn.none.fl_str_mv 15205118
identifier_str_mv 15205118
url https://doi.org/10.1021/jf1011159
http://www.locus.ufv.br/handle/123456789/19436
dc.language.iso.fl_str_mv eng
language eng
dc.relation.ispartofseries.pt-BR.fl_str_mv v. 58, n. 14, p. 8386–8391, July 2010
dc.rights.driver.fl_str_mv American Chemical Society
info:eu-repo/semantics/openAccess
rights_invalid_str_mv American Chemical Society
eu_rights_str_mv openAccess
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dc.publisher.none.fl_str_mv Journal of Agricultural and Food Chemistry
publisher.none.fl_str_mv Journal of Agricultural and Food Chemistry
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