Purification and characterization of a new Xylanase from Humicola grisea var. Thermoidea
Autor(a) principal: | |
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Data de Publicação: | 2004 |
Outros Autores: | |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Journal of Microbiology |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822004000100014 |
Resumo: | The thermophilic fungus Humicola grisea var. thermoidea secretes extracellular xylanase when grown on solid and in liquid media containing wheat bran and banana plant residue as substrates, respectively. At 55ºC, xylanase from the culture filtrate of H. grisea var. thermoidea grown on banana stalk retained 50% of its activity after 28 h of incubation. A xylanase (X2) was isolated from solid state cultures with wheat bran as the carbon source. It was purified to apparent homogeneity by ultrafiltration followed by ion-exchange and hydrophobic interaction chromatography on DEAE-Sepharose and Phenyl-Sepharose resins, respectively. The enzyme had an apparent molecular weight of 29 kDa, as determined by SDS-PAGE. The purified enzyme was most active at pH and temperature ranges of 4.5-6.5 and 55-60ºC, respectively. In addition, X2 showed thermostability at 60ºC with a half-life of approx. 5.5 h. The apparent Km values, using soluble and insoluble arabinoxylans as substrates, were 10.87 and 11.20 mg/ml, respectively. |
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Brazilian Journal of Microbiology |
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Purification and characterization of a new Xylanase from Humicola grisea var. ThermoideaHumicola griseaxylanxylanaseThe thermophilic fungus Humicola grisea var. thermoidea secretes extracellular xylanase when grown on solid and in liquid media containing wheat bran and banana plant residue as substrates, respectively. At 55ºC, xylanase from the culture filtrate of H. grisea var. thermoidea grown on banana stalk retained 50% of its activity after 28 h of incubation. A xylanase (X2) was isolated from solid state cultures with wheat bran as the carbon source. It was purified to apparent homogeneity by ultrafiltration followed by ion-exchange and hydrophobic interaction chromatography on DEAE-Sepharose and Phenyl-Sepharose resins, respectively. The enzyme had an apparent molecular weight of 29 kDa, as determined by SDS-PAGE. The purified enzyme was most active at pH and temperature ranges of 4.5-6.5 and 55-60ºC, respectively. In addition, X2 showed thermostability at 60ºC with a half-life of approx. 5.5 h. The apparent Km values, using soluble and insoluble arabinoxylans as substrates, were 10.87 and 11.20 mg/ml, respectively.Sociedade Brasileira de Microbiologia2004-06-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822004000100014Brazilian Journal of Microbiology v.35 n.1-2 2004reponame:Brazilian Journal of Microbiologyinstname:Sociedade Brasileira de Microbiologia (SBM)instacron:SBM10.1590/S1517-83822004000100014info:eu-repo/semantics/openAccessLucena-Neto,Severino de AlbuquerqueFerreira-Filho,Edivaldo Ximeneseng2004-11-16T00:00:00Zoai:scielo:S1517-83822004000100014Revistahttps://www.scielo.br/j/bjm/ONGhttps://old.scielo.br/oai/scielo-oai.phpbjm@sbmicrobiologia.org.br||mbmartin@usp.br1678-44051517-8382opendoar:2004-11-16T00:00Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM)false |
dc.title.none.fl_str_mv |
Purification and characterization of a new Xylanase from Humicola grisea var. Thermoidea |
title |
Purification and characterization of a new Xylanase from Humicola grisea var. Thermoidea |
spellingShingle |
Purification and characterization of a new Xylanase from Humicola grisea var. Thermoidea Lucena-Neto,Severino de Albuquerque Humicola grisea xylan xylanase |
title_short |
Purification and characterization of a new Xylanase from Humicola grisea var. Thermoidea |
title_full |
Purification and characterization of a new Xylanase from Humicola grisea var. Thermoidea |
title_fullStr |
Purification and characterization of a new Xylanase from Humicola grisea var. Thermoidea |
title_full_unstemmed |
Purification and characterization of a new Xylanase from Humicola grisea var. Thermoidea |
title_sort |
Purification and characterization of a new Xylanase from Humicola grisea var. Thermoidea |
author |
Lucena-Neto,Severino de Albuquerque |
author_facet |
Lucena-Neto,Severino de Albuquerque Ferreira-Filho,Edivaldo Ximenes |
author_role |
author |
author2 |
Ferreira-Filho,Edivaldo Ximenes |
author2_role |
author |
dc.contributor.author.fl_str_mv |
Lucena-Neto,Severino de Albuquerque Ferreira-Filho,Edivaldo Ximenes |
dc.subject.por.fl_str_mv |
Humicola grisea xylan xylanase |
topic |
Humicola grisea xylan xylanase |
description |
The thermophilic fungus Humicola grisea var. thermoidea secretes extracellular xylanase when grown on solid and in liquid media containing wheat bran and banana plant residue as substrates, respectively. At 55ºC, xylanase from the culture filtrate of H. grisea var. thermoidea grown on banana stalk retained 50% of its activity after 28 h of incubation. A xylanase (X2) was isolated from solid state cultures with wheat bran as the carbon source. It was purified to apparent homogeneity by ultrafiltration followed by ion-exchange and hydrophobic interaction chromatography on DEAE-Sepharose and Phenyl-Sepharose resins, respectively. The enzyme had an apparent molecular weight of 29 kDa, as determined by SDS-PAGE. The purified enzyme was most active at pH and temperature ranges of 4.5-6.5 and 55-60ºC, respectively. In addition, X2 showed thermostability at 60ºC with a half-life of approx. 5.5 h. The apparent Km values, using soluble and insoluble arabinoxylans as substrates, were 10.87 and 11.20 mg/ml, respectively. |
publishDate |
2004 |
dc.date.none.fl_str_mv |
2004-06-01 |
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=S1517-83822004000100014 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822004000100014 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1517-83822004000100014 |
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 |
Sociedade Brasileira de Microbiologia |
publisher.none.fl_str_mv |
Sociedade Brasileira de Microbiologia |
dc.source.none.fl_str_mv |
Brazilian Journal of Microbiology v.35 n.1-2 2004 reponame:Brazilian Journal of Microbiology instname:Sociedade Brasileira de Microbiologia (SBM) instacron:SBM |
instname_str |
Sociedade Brasileira de Microbiologia (SBM) |
instacron_str |
SBM |
institution |
SBM |
reponame_str |
Brazilian Journal of Microbiology |
collection |
Brazilian Journal of Microbiology |
repository.name.fl_str_mv |
Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM) |
repository.mail.fl_str_mv |
bjm@sbmicrobiologia.org.br||mbmartin@usp.br |
_version_ |
1752122200077369344 |