Production and Characterization of β-Glucanase Secreted by the Yeast Kluyveromyces marxianus
Autor(a) principal: | |
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Data de Publicação: | 2014 |
Outros Autores: | , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | LOCUS Repositório Institucional da UFV |
Texto Completo: | http://dx.doi.org/10.1007/s12010-013-0683-3 http://www.locus.ufv.br/handle/123456789/12908 |
Resumo: | An extracellular β-glucanase secreted by Kluyveromyces marxianus was identified for the first time. The optimal conditions for the production of this enzyme were evaluated by response surface methodology. The optimal conditions to produce β-glucanase were a glucose concentration of 4 % (w/v), a pH of 5.5, and an incubation temperature of 35 °C. Response surface methodology was also used to determine the pH and temperature required for the optimal enzymatic activity. The highest enzyme activity was obtained at a pH of 5.5 and a temperature of 55 °C. Furthermore, the enzyme was partially purified and sequenced, and its specificity for different substrates was evaluated. The results suggest that the enzyme is an endo-β-1,3(4)-glucanase. After optimizing the conditions for β-glucanase production, the culture supernatant was found to be effective in digesting the cell wall of the yeast Saccharomyces cerevisiae, showing the great potential of β-glucanase in the biotechnological production of soluble β-glucan. |
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Lopes, Mariana R.Souza, Carlos J. A. deRodrigues, Marina Q. R. B.Costa, Daniela A.Santos, Ancély F. dosOliveira, Leandro L. deRamos, Humberto J. O.Guimarães, Valéria M.Silveira, Wendel B.Passos, Flávia M. L.Fietto, Luciano G.2017-11-08T15:55:09Z2017-11-08T15:55:09Z2014-01-041559-0291http://dx.doi.org/10.1007/s12010-013-0683-3http://www.locus.ufv.br/handle/123456789/12908An extracellular β-glucanase secreted by Kluyveromyces marxianus was identified for the first time. The optimal conditions for the production of this enzyme were evaluated by response surface methodology. The optimal conditions to produce β-glucanase were a glucose concentration of 4 % (w/v), a pH of 5.5, and an incubation temperature of 35 °C. Response surface methodology was also used to determine the pH and temperature required for the optimal enzymatic activity. The highest enzyme activity was obtained at a pH of 5.5 and a temperature of 55 °C. Furthermore, the enzyme was partially purified and sequenced, and its specificity for different substrates was evaluated. The results suggest that the enzyme is an endo-β-1,3(4)-glucanase. After optimizing the conditions for β-glucanase production, the culture supernatant was found to be effective in digesting the cell wall of the yeast Saccharomyces cerevisiae, showing the great potential of β-glucanase in the biotechnological production of soluble β-glucan.engApplied Biochemistry and BiotechnologyVolume 172, Issue 5, p. 2412–2424, March 2014β-glucanaseKluyveromyces marxianusProductionOptimizationYeast lysisProduction and Characterization of β-Glucanase Secreted by the Yeast Kluyveromyces marxianusinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfinfo:eu-repo/semantics/openAccessreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFVORIGINAL10.1007-s12010-013-0683-3.pdf10.1007-s12010-013-0683-3.pdftexto completoapplication/pdf978011https://locus.ufv.br//bitstream/123456789/12908/1/10.1007-s12010-013-0683-3.pdf97e7688caef83213b10cd63432a42f6aMD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://locus.ufv.br//bitstream/123456789/12908/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52THUMBNAIL10.1007-s12010-013-0683-3.pdf.jpg10.1007-s12010-013-0683-3.pdf.jpgIM Thumbnailimage/jpeg4860https://locus.ufv.br//bitstream/123456789/12908/3/10.1007-s12010-013-0683-3.pdf.jpgecf4dd307a82b8951c7d3a13b4d23815MD53123456789/129082017-11-08 22:01:01.577oai:locus.ufv.br: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Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452017-11-09T01:01:01LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false |
dc.title.en.fl_str_mv |
Production and Characterization of β-Glucanase Secreted by the Yeast Kluyveromyces marxianus |
title |
Production and Characterization of β-Glucanase Secreted by the Yeast Kluyveromyces marxianus |
spellingShingle |
Production and Characterization of β-Glucanase Secreted by the Yeast Kluyveromyces marxianus Lopes, Mariana R. β-glucanase Kluyveromyces marxianus Production Optimization Yeast lysis |
title_short |
Production and Characterization of β-Glucanase Secreted by the Yeast Kluyveromyces marxianus |
title_full |
Production and Characterization of β-Glucanase Secreted by the Yeast Kluyveromyces marxianus |
title_fullStr |
Production and Characterization of β-Glucanase Secreted by the Yeast Kluyveromyces marxianus |
title_full_unstemmed |
Production and Characterization of β-Glucanase Secreted by the Yeast Kluyveromyces marxianus |
title_sort |
Production and Characterization of β-Glucanase Secreted by the Yeast Kluyveromyces marxianus |
author |
Lopes, Mariana R. |
author_facet |
Lopes, Mariana R. Souza, Carlos J. A. de Rodrigues, Marina Q. R. B. Costa, Daniela A. Santos, Ancély F. dos Oliveira, Leandro L. de Ramos, Humberto J. O. Guimarães, Valéria M. Silveira, Wendel B. Passos, Flávia M. L. Fietto, Luciano G. |
author_role |
author |
author2 |
Souza, Carlos J. A. de Rodrigues, Marina Q. R. B. Costa, Daniela A. Santos, Ancély F. dos Oliveira, Leandro L. de Ramos, Humberto J. O. Guimarães, Valéria M. Silveira, Wendel B. Passos, Flávia M. L. Fietto, Luciano G. |
author2_role |
author author author author author author author author author author |
dc.contributor.author.fl_str_mv |
Lopes, Mariana R. Souza, Carlos J. A. de Rodrigues, Marina Q. R. B. Costa, Daniela A. Santos, Ancély F. dos Oliveira, Leandro L. de Ramos, Humberto J. O. Guimarães, Valéria M. Silveira, Wendel B. Passos, Flávia M. L. Fietto, Luciano G. |
dc.subject.pt-BR.fl_str_mv |
β-glucanase Kluyveromyces marxianus Production Optimization Yeast lysis |
topic |
β-glucanase Kluyveromyces marxianus Production Optimization Yeast lysis |
description |
An extracellular β-glucanase secreted by Kluyveromyces marxianus was identified for the first time. The optimal conditions for the production of this enzyme were evaluated by response surface methodology. The optimal conditions to produce β-glucanase were a glucose concentration of 4 % (w/v), a pH of 5.5, and an incubation temperature of 35 °C. Response surface methodology was also used to determine the pH and temperature required for the optimal enzymatic activity. The highest enzyme activity was obtained at a pH of 5.5 and a temperature of 55 °C. Furthermore, the enzyme was partially purified and sequenced, and its specificity for different substrates was evaluated. The results suggest that the enzyme is an endo-β-1,3(4)-glucanase. After optimizing the conditions for β-glucanase production, the culture supernatant was found to be effective in digesting the cell wall of the yeast Saccharomyces cerevisiae, showing the great potential of β-glucanase in the biotechnological production of soluble β-glucan. |
publishDate |
2014 |
dc.date.issued.fl_str_mv |
2014-01-04 |
dc.date.accessioned.fl_str_mv |
2017-11-08T15:55:09Z |
dc.date.available.fl_str_mv |
2017-11-08T15:55:09Z |
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 |
http://dx.doi.org/10.1007/s12010-013-0683-3 http://www.locus.ufv.br/handle/123456789/12908 |
dc.identifier.issn.none.fl_str_mv |
1559-0291 |
identifier_str_mv |
1559-0291 |
url |
http://dx.doi.org/10.1007/s12010-013-0683-3 http://www.locus.ufv.br/handle/123456789/12908 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartofseries.pt-BR.fl_str_mv |
Volume 172, Issue 5, p. 2412–2424, March 2014 |
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info:eu-repo/semantics/openAccess |
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openAccess |
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Applied Biochemistry and Biotechnology |
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Applied Biochemistry and Biotechnology |
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