Coexpression of rumen fungal xylanase and bifunctional cellulase genes in Escherichia coli
Autor(a) principal: | |
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Data de Publicação: | 2017 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Archives of Biology and Technology |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132017000100407 |
Resumo: | ABSTRACT Rumen fungi inhabit the gastro-intestinal tract of ruminants and the most non-ruminant herbivores. Rumen fungi produce highly active plant cell wall degrading enzymes, therefore they have gained scientific interest. In this study, genes encoding xylanase (xynA-7) and cellulase (celA-5) were amplified from Neocallimastix sp. GMLF7 and Orpinomyces sp. GMLF5, respectively, and expressed in Escherichia coli. XynA-7 was found to be active only on xylan, however CelA-5 had activity both on carboxymethyl cellulose and lichenan. Lichenase activity of CelA-5 was found to be higher than carboxymethyl cellulase activity. The optimal conditions were at pH 6.0 and 40 °C for CelA-5 and at pH 6.5 and 50 °C for XynA-7. A coexpression vector was constructed to coproduce the XynA-7 and CelA-5 and then transformed into E. coli. The ability of the transformed E. coli strain to produce CMCase, xylanase and lichenase was evaluated. The transformed E. coli strain acquired the capacity to degrade CMC, xylan and lichenan. |
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Brazilian Archives of Biology and Technology |
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Coexpression of rumen fungal xylanase and bifunctional cellulase genes in Escherichia coliRumen fungixylanasecellulasecoexpressionE. coliABSTRACT Rumen fungi inhabit the gastro-intestinal tract of ruminants and the most non-ruminant herbivores. Rumen fungi produce highly active plant cell wall degrading enzymes, therefore they have gained scientific interest. In this study, genes encoding xylanase (xynA-7) and cellulase (celA-5) were amplified from Neocallimastix sp. GMLF7 and Orpinomyces sp. GMLF5, respectively, and expressed in Escherichia coli. XynA-7 was found to be active only on xylan, however CelA-5 had activity both on carboxymethyl cellulose and lichenan. Lichenase activity of CelA-5 was found to be higher than carboxymethyl cellulase activity. The optimal conditions were at pH 6.0 and 40 °C for CelA-5 and at pH 6.5 and 50 °C for XynA-7. A coexpression vector was constructed to coproduce the XynA-7 and CelA-5 and then transformed into E. coli. The ability of the transformed E. coli strain to produce CMCase, xylanase and lichenase was evaluated. The transformed E. coli strain acquired the capacity to degrade CMC, xylan and lichenan.Instituto de Tecnologia do Paraná - Tecpar2017-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132017000100407Brazilian Archives of Biology and Technology v.60 2017reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/1678-4324-2017160462info:eu-repo/semantics/openAccessComlekcioglu,UgurGunes,MervaAltun,HanifiEkiz,Dilek OzgunAygan,Ashabileng2017-05-15T00:00:00Zoai:scielo:S1516-89132017000100407Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2017-05-15T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false |
dc.title.none.fl_str_mv |
Coexpression of rumen fungal xylanase and bifunctional cellulase genes in Escherichia coli |
title |
Coexpression of rumen fungal xylanase and bifunctional cellulase genes in Escherichia coli |
spellingShingle |
Coexpression of rumen fungal xylanase and bifunctional cellulase genes in Escherichia coli Comlekcioglu,Ugur Rumen fungi xylanase cellulase coexpression E. coli |
title_short |
Coexpression of rumen fungal xylanase and bifunctional cellulase genes in Escherichia coli |
title_full |
Coexpression of rumen fungal xylanase and bifunctional cellulase genes in Escherichia coli |
title_fullStr |
Coexpression of rumen fungal xylanase and bifunctional cellulase genes in Escherichia coli |
title_full_unstemmed |
Coexpression of rumen fungal xylanase and bifunctional cellulase genes in Escherichia coli |
title_sort |
Coexpression of rumen fungal xylanase and bifunctional cellulase genes in Escherichia coli |
author |
Comlekcioglu,Ugur |
author_facet |
Comlekcioglu,Ugur Gunes,Merva Altun,Hanifi Ekiz,Dilek Ozgun Aygan,Ashabil |
author_role |
author |
author2 |
Gunes,Merva Altun,Hanifi Ekiz,Dilek Ozgun Aygan,Ashabil |
author2_role |
author author author author |
dc.contributor.author.fl_str_mv |
Comlekcioglu,Ugur Gunes,Merva Altun,Hanifi Ekiz,Dilek Ozgun Aygan,Ashabil |
dc.subject.por.fl_str_mv |
Rumen fungi xylanase cellulase coexpression E. coli |
topic |
Rumen fungi xylanase cellulase coexpression E. coli |
description |
ABSTRACT Rumen fungi inhabit the gastro-intestinal tract of ruminants and the most non-ruminant herbivores. Rumen fungi produce highly active plant cell wall degrading enzymes, therefore they have gained scientific interest. In this study, genes encoding xylanase (xynA-7) and cellulase (celA-5) were amplified from Neocallimastix sp. GMLF7 and Orpinomyces sp. GMLF5, respectively, and expressed in Escherichia coli. XynA-7 was found to be active only on xylan, however CelA-5 had activity both on carboxymethyl cellulose and lichenan. Lichenase activity of CelA-5 was found to be higher than carboxymethyl cellulase activity. The optimal conditions were at pH 6.0 and 40 °C for CelA-5 and at pH 6.5 and 50 °C for XynA-7. A coexpression vector was constructed to coproduce the XynA-7 and CelA-5 and then transformed into E. coli. The ability of the transformed E. coli strain to produce CMCase, xylanase and lichenase was evaluated. The transformed E. coli strain acquired the capacity to degrade CMC, xylan and lichenan. |
publishDate |
2017 |
dc.date.none.fl_str_mv |
2017-01-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132017000100407 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132017000100407 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/1678-4324-2017160462 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Instituto de Tecnologia do Paraná - Tecpar |
publisher.none.fl_str_mv |
Instituto de Tecnologia do Paraná - Tecpar |
dc.source.none.fl_str_mv |
Brazilian Archives of Biology and Technology v.60 2017 reponame:Brazilian Archives of Biology and Technology instname:Instituto de Tecnologia do Paraná (Tecpar) instacron:TECPAR |
instname_str |
Instituto de Tecnologia do Paraná (Tecpar) |
instacron_str |
TECPAR |
institution |
TECPAR |
reponame_str |
Brazilian Archives of Biology and Technology |
collection |
Brazilian Archives of Biology and Technology |
repository.name.fl_str_mv |
Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar) |
repository.mail.fl_str_mv |
babt@tecpar.br||babt@tecpar.br |
_version_ |
1750318278125813760 |