Characterization of an exoinulinase produced by Aspergillus terreus CCT 4083 grown on sugar cane bagasse
Autor(a) principal: | |
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Data de Publicação: | 2010 |
Outros Autores: | , , , , |
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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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 |
format |
article |
status_str |
publishedVersion |
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 |
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American Chemical Society |
eu_rights_str_mv |
openAccess |
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application/pdf |
dc.publisher.none.fl_str_mv |
Journal of Agricultural and Food Chemistry |
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Journal of Agricultural and Food Chemistry |
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