Produção de uma xilanase recombinante de Streptomyces sp. S27 e aplicações biotecnológicas
Autor(a) principal: | |
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Data de Publicação: | 2016 |
Tipo de documento: | Tese |
Idioma: | por |
Título da fonte: | Repositório Institucional da UFG |
Texto Completo: | http://repositorio.bc.ufg.br/tede/handle/tede/6865 |
Resumo: | The xylan-degrading enzymes are responsible for the hydrolysis of xylan and can be produced by a variety of microorganisms such as bacteria and fungi. Bacteria produce an effective xylanolytic system composed of endoxylanase, β-xylosidases, arabinofuronosidases, glucuronidases, acetyl xylan esterase and esterase ferulic acid and have been the target of several studies on the production and application of these enzymes in biotechnological processes such as hydrolysis of different substrates to obtain fermentable sugars. Actinomycetes comprising a phylum Gram positive, aerobic, which generally form branched filaments, often in the form of mycelium. Among the actinomycetes, bacteria of the genus Streptomyces in particular, have been studied due to their important role biotechnology. In the present study, we report the expression, purification and characterization of xylanase (XynBS27) recombinantly in yeast P. pastoris. To achieve high levels of production, the gene was designed and synthesized by optimizing codon usage for P. pastoris. The synthetic gene (xynBS27) was cloned into expression vector containing the AOXI promoter followed by integration into the yeast genome. The increased production of XynBS27 was after 96 h of induction, 2% methanol at 28 °C and 200 rpm (80 U/mL), the enzyme was purified in one chromatography step molecular exclusion obtained specific activity of 8525 U/ mg its highest activity at 75 °C and pH 6, it is thermostable and showed stability at pH 5, 6 and 7. The XynBS27 has a molecular mass of 19 kDa active in zymography. Many ions were tested Al3+, NH4+, Ba2+ and Mg2+ were inducers and Ag+ ions, Hg2+ and Cu2+ inhibited, the sulfides of Mn2+, Zn2+, Fe3+ and denaturing agents EDTA and SDS inhibited XynBS27. The enzyme is tolerant to high concentrations of glucose and xylose. The Km and Vmax values were 12.38 mg/mL, 13.679 mmol/(min.mL), respectively, Ki of 180 mM competitive inhibition. The use of the enzyme in baking has proved very promising in the evaluated parameters, volume, density, reducing sugar, stiffness, consistency, firmness and water retention. |
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Ulhoa, Cirano Joséhttp://lattes.cnpq.br/8368469162867277Bataus, Luiz Artur Mendeshttp://lattes.cnpq.br/5637230378599476Faria, Fabricia Paula deGeorg, Raphaela de CastroColussi, FrancieliSteindorff, Andrei SteccaUlhoa, Cirano Joséhttp://lattes.cnpq.br/3556341716515132Cunha, Carolina Cândida de Queiroz Brito2017-02-22T13:08:29Z2016-12-19BRITO-CUNHA, C. C. Q. Produção de uma xilanase recombinante de Streptomyces sp. S27 e aplicações biotecnológicas. 2016. 133 f. Tese (Doutorado em Biologia) - Universidade Federal de Goiás, Goiânia, 2016.http://repositorio.bc.ufg.br/tede/handle/tede/6865The xylan-degrading enzymes are responsible for the hydrolysis of xylan and can be produced by a variety of microorganisms such as bacteria and fungi. Bacteria produce an effective xylanolytic system composed of endoxylanase, β-xylosidases, arabinofuronosidases, glucuronidases, acetyl xylan esterase and esterase ferulic acid and have been the target of several studies on the production and application of these enzymes in biotechnological processes such as hydrolysis of different substrates to obtain fermentable sugars. Actinomycetes comprising a phylum Gram positive, aerobic, which generally form branched filaments, often in the form of mycelium. Among the actinomycetes, bacteria of the genus Streptomyces in particular, have been studied due to their important role biotechnology. In the present study, we report the expression, purification and characterization of xylanase (XynBS27) recombinantly in yeast P. pastoris. To achieve high levels of production, the gene was designed and synthesized by optimizing codon usage for P. pastoris. The synthetic gene (xynBS27) was cloned into expression vector containing the AOXI promoter followed by integration into the yeast genome. The increased production of XynBS27 was after 96 h of induction, 2% methanol at 28 °C and 200 rpm (80 U/mL), the enzyme was purified in one chromatography step molecular exclusion obtained specific activity of 8525 U/ mg its highest activity at 75 °C and pH 6, it is thermostable and showed stability at pH 5, 6 and 7. The XynBS27 has a molecular mass of 19 kDa active in zymography. Many ions were tested Al3+, NH4+, Ba2+ and Mg2+ were inducers and Ag+ ions, Hg2+ and Cu2+ inhibited, the sulfides of Mn2+, Zn2+, Fe3+ and denaturing agents EDTA and SDS inhibited XynBS27. The enzyme is tolerant to high concentrations of glucose and xylose. The Km and Vmax values were 12.38 mg/mL, 13.679 mmol/(min.mL), respectively, Ki of 180 mM competitive inhibition. The use of the enzyme in baking has proved very promising in the evaluated parameters, volume, density, reducing sugar, stiffness, consistency, firmness and water retention.As enzimas xilanolíticas são responsáveis pela hidrólise da xilana e podem ser produzidas por uma variedade de micro-organismos como bactérias e fungos. As bactérias produzem um eficiente sistema xilanolítico composto de endoxilanases, β-xilosidases, arabinofuranosidases, glucuronidases, acetil xilana esterase e ácido ferúlico esterase e tem sido alvo de diversos estudos sobre a produção e aplicação destas enzimas em processos biotecnológicos, como a hidrólise de diferentes substratos para obtenção de açúcares fermentáveis. Entre os actinomicetos, as bactérias do gênero Streptomyces em particular, têm sido estudadas devido ao seu importante papel biotecnológico. No presente estudo, é relatada a expressão do gene, purificação e caracterização da xilanase (XynBS27) recombinante pela levedura P. pastoris. Para alcançar altos níveis de produção, o gene foi desenhado e sintetizado, otimizando o códon usage para P. pastoris. O gene sintético (xynBS27) foi clonado em vetor de expressão contendo o promotor AOXI, seguindo-se da integração no genoma da levedura. A maior produção da XynBS27 foi obtida após 96 h de indução, 2% de metanol, à 28 ºC e 200 r.p.m. (80 U/mL), a enzima foi purificada por de cromatografia de exclusão molecular, apresentando atividade específica de 8525 U/mg, sua maior atividade foi a 75 ºC e pH 6, se mostrou termo estável e apresentou estabilidade em pH 5, 6 e 7. A XynBS27 apresenta massa molecular de 19 kDa é ativa em zimograma. Diversos íons foram testados, sendo o Al3+, NH4+, Ba2+ e o Mg2+ indutores e os íons Ag+, Hg2+ e Cu2+ inibidores, os sulfetos de Mn2+, Zn2+, Fe3+ e os agentes desnaturantes EDTA e SDS também inibiram a XynBS27. A enzima é tolerante à altas concentrações de glicose e xilose. Os valores de Km e Vmáx foram 12,38 mg/mL e 13,679 µmol/(min.mL), respectivamente em xilana, Ki de 180 mM de xilose, indicando inibição competitiva. A utilização da enzima na panificação mostrou-se muito promissora em relação aos parâmetros avaliados, volume, densidade, açúcar redutor, rigidez, consistência, firmeza e retenção de água.Submitted by Cássia Santos (cassia.bcufg@gmail.com) on 2017-02-22T10:55:05Z No. of bitstreams: 2 Tese - Carolina Cândida de Queiroz Brito Cunha - 2016.pdf: 2598077 bytes, checksum: fc0189e22f130ec24f122de4f57a3c02 (MD5) license_rdf: 0 bytes, checksum: d41d8cd98f00b204e9800998ecf8427e (MD5)Approved for entry into archive by Luciana Ferreira (lucgeral@gmail.com) on 2017-02-22T13:08:29Z (GMT) No. of bitstreams: 2 Tese - Carolina Cândida de Queiroz Brito Cunha - 2016.pdf: 2598077 bytes, checksum: fc0189e22f130ec24f122de4f57a3c02 (MD5) license_rdf: 0 bytes, checksum: d41d8cd98f00b204e9800998ecf8427e (MD5)Made available in DSpace on 2017-02-22T13:08:29Z (GMT). No. of bitstreams: 2 Tese - Carolina Cândida de Queiroz Brito Cunha - 2016.pdf: 2598077 bytes, checksum: fc0189e22f130ec24f122de4f57a3c02 (MD5) license_rdf: 0 bytes, checksum: d41d8cd98f00b204e9800998ecf8427e (MD5) Previous issue date: 2016-12-19Outroapplication/pdfporUniversidade Federal de GoiásPrograma de Pós-graduação em Biologia (ICB)UFGBrasilInstituto de Ciências Biológicas - ICB (RG)http://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessXilanaseStreptomycesP. pastorisExpressão heterólogaTermoestávelPanificaçãoXylanaseStreptomycesP. pastorisHeterologous expressionThermostableBakeryCIENCIAS BIOLOGICAS::BIOQUIMICACIENCIAS BIOLOGICAS::GENETICAProdução de uma xilanase recombinante de Streptomyces sp. S27 e aplicações biotecnológicasImprovement of bread-making quality by supplementation with a recombinant xylanase from Streptomyces sp. 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dc.title.por.fl_str_mv |
Produção de uma xilanase recombinante de Streptomyces sp. S27 e aplicações biotecnológicas |
dc.title.alternative.eng.fl_str_mv |
Improvement of bread-making quality by supplementation with a recombinant xylanase from Streptomyces sp. S27 |
title |
Produção de uma xilanase recombinante de Streptomyces sp. S27 e aplicações biotecnológicas |
spellingShingle |
Produção de uma xilanase recombinante de Streptomyces sp. S27 e aplicações biotecnológicas Cunha, Carolina Cândida de Queiroz Brito Xilanase Streptomyces P. pastoris Expressão heteróloga Termoestável Panificação Xylanase Streptomyces P. pastoris Heterologous expression Thermostable Bakery CIENCIAS BIOLOGICAS::BIOQUIMICA CIENCIAS BIOLOGICAS::GENETICA |
title_short |
Produção de uma xilanase recombinante de Streptomyces sp. S27 e aplicações biotecnológicas |
title_full |
Produção de uma xilanase recombinante de Streptomyces sp. S27 e aplicações biotecnológicas |
title_fullStr |
Produção de uma xilanase recombinante de Streptomyces sp. S27 e aplicações biotecnológicas |
title_full_unstemmed |
Produção de uma xilanase recombinante de Streptomyces sp. S27 e aplicações biotecnológicas |
title_sort |
Produção de uma xilanase recombinante de Streptomyces sp. S27 e aplicações biotecnológicas |
author |
Cunha, Carolina Cândida de Queiroz Brito |
author_facet |
Cunha, Carolina Cândida de Queiroz Brito |
author_role |
author |
dc.contributor.advisor1.fl_str_mv |
Ulhoa, Cirano José |
dc.contributor.advisor1Lattes.fl_str_mv |
http://lattes.cnpq.br/8368469162867277 |
dc.contributor.advisor-co1.fl_str_mv |
Bataus, Luiz Artur Mendes |
dc.contributor.advisor-co1Lattes.fl_str_mv |
http://lattes.cnpq.br/5637230378599476 |
dc.contributor.referee1.fl_str_mv |
Faria, Fabricia Paula de |
dc.contributor.referee2.fl_str_mv |
Georg, Raphaela de Castro |
dc.contributor.referee3.fl_str_mv |
Colussi, Francieli |
dc.contributor.referee4.fl_str_mv |
Steindorff, Andrei Stecca |
dc.contributor.referee5.fl_str_mv |
Ulhoa, Cirano José |
dc.contributor.authorLattes.fl_str_mv |
http://lattes.cnpq.br/3556341716515132 |
dc.contributor.author.fl_str_mv |
Cunha, Carolina Cândida de Queiroz Brito |
contributor_str_mv |
Ulhoa, Cirano José Bataus, Luiz Artur Mendes Faria, Fabricia Paula de Georg, Raphaela de Castro Colussi, Francieli Steindorff, Andrei Stecca Ulhoa, Cirano José |
dc.subject.por.fl_str_mv |
Xilanase Streptomyces P. pastoris Expressão heteróloga Termoestável Panificação |
topic |
Xilanase Streptomyces P. pastoris Expressão heteróloga Termoestável Panificação Xylanase Streptomyces P. pastoris Heterologous expression Thermostable Bakery CIENCIAS BIOLOGICAS::BIOQUIMICA CIENCIAS BIOLOGICAS::GENETICA |
dc.subject.eng.fl_str_mv |
Xylanase Streptomyces P. pastoris Heterologous expression Thermostable Bakery |
dc.subject.cnpq.fl_str_mv |
CIENCIAS BIOLOGICAS::BIOQUIMICA CIENCIAS BIOLOGICAS::GENETICA |
description |
The xylan-degrading enzymes are responsible for the hydrolysis of xylan and can be produced by a variety of microorganisms such as bacteria and fungi. Bacteria produce an effective xylanolytic system composed of endoxylanase, β-xylosidases, arabinofuronosidases, glucuronidases, acetyl xylan esterase and esterase ferulic acid and have been the target of several studies on the production and application of these enzymes in biotechnological processes such as hydrolysis of different substrates to obtain fermentable sugars. Actinomycetes comprising a phylum Gram positive, aerobic, which generally form branched filaments, often in the form of mycelium. Among the actinomycetes, bacteria of the genus Streptomyces in particular, have been studied due to their important role biotechnology. In the present study, we report the expression, purification and characterization of xylanase (XynBS27) recombinantly in yeast P. pastoris. To achieve high levels of production, the gene was designed and synthesized by optimizing codon usage for P. pastoris. The synthetic gene (xynBS27) was cloned into expression vector containing the AOXI promoter followed by integration into the yeast genome. The increased production of XynBS27 was after 96 h of induction, 2% methanol at 28 °C and 200 rpm (80 U/mL), the enzyme was purified in one chromatography step molecular exclusion obtained specific activity of 8525 U/ mg its highest activity at 75 °C and pH 6, it is thermostable and showed stability at pH 5, 6 and 7. The XynBS27 has a molecular mass of 19 kDa active in zymography. Many ions were tested Al3+, NH4+, Ba2+ and Mg2+ were inducers and Ag+ ions, Hg2+ and Cu2+ inhibited, the sulfides of Mn2+, Zn2+, Fe3+ and denaturing agents EDTA and SDS inhibited XynBS27. The enzyme is tolerant to high concentrations of glucose and xylose. The Km and Vmax values were 12.38 mg/mL, 13.679 mmol/(min.mL), respectively, Ki of 180 mM competitive inhibition. The use of the enzyme in baking has proved very promising in the evaluated parameters, volume, density, reducing sugar, stiffness, consistency, firmness and water retention. |
publishDate |
2016 |
dc.date.issued.fl_str_mv |
2016-12-19 |
dc.date.accessioned.fl_str_mv |
2017-02-22T13:08:29Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/doctoralThesis |
format |
doctoralThesis |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
BRITO-CUNHA, C. C. Q. Produção de uma xilanase recombinante de Streptomyces sp. S27 e aplicações biotecnológicas. 2016. 133 f. Tese (Doutorado em Biologia) - Universidade Federal de Goiás, Goiânia, 2016. |
dc.identifier.uri.fl_str_mv |
http://repositorio.bc.ufg.br/tede/handle/tede/6865 |
identifier_str_mv |
BRITO-CUNHA, C. C. Q. Produção de uma xilanase recombinante de Streptomyces sp. S27 e aplicações biotecnológicas. 2016. 133 f. Tese (Doutorado em Biologia) - Universidade Federal de Goiás, Goiânia, 2016. |
url |
http://repositorio.bc.ufg.br/tede/handle/tede/6865 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.relation.program.fl_str_mv |
6883982777473437920 |
dc.relation.confidence.fl_str_mv |
600 600 600 600 600 |
dc.relation.department.fl_str_mv |
-3872772117827373404 |
dc.relation.cnpq.fl_str_mv |
893477990329266114 -5518144268585252051 |
dc.relation.sponsorship.fl_str_mv |
2442915598251853972 |
dc.rights.driver.fl_str_mv |
http://creativecommons.org/licenses/by-nc-nd/4.0/ info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by-nc-nd/4.0/ |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Universidade Federal de Goiás |
dc.publisher.program.fl_str_mv |
Programa de Pós-graduação em Biologia (ICB) |
dc.publisher.initials.fl_str_mv |
UFG |
dc.publisher.country.fl_str_mv |
Brasil |
dc.publisher.department.fl_str_mv |
Instituto de Ciências Biológicas - ICB (RG) |
publisher.none.fl_str_mv |
Universidade Federal de Goiás |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da UFG instname:Universidade Federal de Goiás (UFG) instacron:UFG |
instname_str |
Universidade Federal de Goiás (UFG) |
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UFG |
institution |
UFG |
reponame_str |
Repositório Institucional da UFG |
collection |
Repositório Institucional da UFG |
bitstream.url.fl_str_mv |
http://repositorio.bc.ufg.br/tede/bitstreams/27ea6d87-d6e1-4316-ab3d-100fc04a816f/download http://repositorio.bc.ufg.br/tede/bitstreams/7801f9b3-f1fd-41ab-8e72-9f45c703a8d3/download http://repositorio.bc.ufg.br/tede/bitstreams/7c980c70-0818-4626-a058-5f3c5a5d48c4/download http://repositorio.bc.ufg.br/tede/bitstreams/9da75843-2f22-4d6c-9d83-f3ac1e551540/download http://repositorio.bc.ufg.br/tede/bitstreams/24c70508-691a-4feb-8d22-f3b38b43a754/download |
bitstream.checksum.fl_str_mv |
bd3efa91386c1718a7f26a329fdcb468 4afdbb8c545fd630ea7db775da747b2f d41d8cd98f00b204e9800998ecf8427e d41d8cd98f00b204e9800998ecf8427e fc0189e22f130ec24f122de4f57a3c02 |
bitstream.checksumAlgorithm.fl_str_mv |
MD5 MD5 MD5 MD5 MD5 |
repository.name.fl_str_mv |
Repositório Institucional da UFG - Universidade Federal de Goiás (UFG) |
repository.mail.fl_str_mv |
tasesdissertacoes.bc@ufg.br |
_version_ |
1798044338110857216 |