Nuclease p1 immobilized on deae cellulose
Autor(a) principal: | |
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Data de Publicação: | 2010 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Journal of Chemical Engineering |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322010000100003 |
Resumo: | Effects of various factors, such as pH, ionic strength, glutaraldehyde concentration, enzyme amount and immobilization time, on enzyme activity were investigated. The immobilization conditions were optimized by orthogonal experiments. Characterizations of immobilized nuclease p1 were also evaluated. Through orthogonal optimization, the optimal immobilization conditions were as follows: pH 5.6, ionic strength 0.125, glutaraldehyde concentration 0.20% and immobilization time 2.0 h. Optimal pH of immobilized enzyme was 5.8. Optimal temperature of immobilized enzyme was 70ºC. Thermal, operational and storage stabilities of the enzyme were improved after it was immobilized on DEAE cellulose. Michaelis constant Km of immobilized enzyme at 69ºC was found to be 27.21 g/l by the Lineweaver-Burk plot. |
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Brazilian Journal of Chemical Engineering |
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Nuclease p1 immobilized on deae celluloseDEAE celluloseNuclease p1ImmobilizationCharacterizationEffects of various factors, such as pH, ionic strength, glutaraldehyde concentration, enzyme amount and immobilization time, on enzyme activity were investigated. The immobilization conditions were optimized by orthogonal experiments. Characterizations of immobilized nuclease p1 were also evaluated. Through orthogonal optimization, the optimal immobilization conditions were as follows: pH 5.6, ionic strength 0.125, glutaraldehyde concentration 0.20% and immobilization time 2.0 h. Optimal pH of immobilized enzyme was 5.8. Optimal temperature of immobilized enzyme was 70ºC. Thermal, operational and storage stabilities of the enzyme were improved after it was immobilized on DEAE cellulose. Michaelis constant Km of immobilized enzyme at 69ºC was found to be 27.21 g/l by the Lineweaver-Burk plot.Brazilian Society of Chemical Engineering2010-03-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322010000100003Brazilian Journal of Chemical Engineering v.27 n.1 2010reponame:Brazilian Journal of Chemical Engineeringinstname:Associação Brasileira de Engenharia Química (ABEQ)instacron:ABEQ10.1590/S0104-66322010000100003info:eu-repo/semantics/openAccessShi,Lu-EYi,YuTang,Zhen-XingXiong,Wen-YueMei,Jiang-FengYing,Guo-Qingeng2010-04-14T00:00:00Zoai:scielo:S0104-66322010000100003Revistahttps://www.scielo.br/j/bjce/https://old.scielo.br/oai/scielo-oai.phprgiudici@usp.br||rgiudici@usp.br1678-43830104-6632opendoar:2010-04-14T00:00Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)false |
dc.title.none.fl_str_mv |
Nuclease p1 immobilized on deae cellulose |
title |
Nuclease p1 immobilized on deae cellulose |
spellingShingle |
Nuclease p1 immobilized on deae cellulose Shi,Lu-E DEAE cellulose Nuclease p1 Immobilization Characterization |
title_short |
Nuclease p1 immobilized on deae cellulose |
title_full |
Nuclease p1 immobilized on deae cellulose |
title_fullStr |
Nuclease p1 immobilized on deae cellulose |
title_full_unstemmed |
Nuclease p1 immobilized on deae cellulose |
title_sort |
Nuclease p1 immobilized on deae cellulose |
author |
Shi,Lu-E |
author_facet |
Shi,Lu-E Yi,Yu Tang,Zhen-Xing Xiong,Wen-Yue Mei,Jiang-Feng Ying,Guo-Qing |
author_role |
author |
author2 |
Yi,Yu Tang,Zhen-Xing Xiong,Wen-Yue Mei,Jiang-Feng Ying,Guo-Qing |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Shi,Lu-E Yi,Yu Tang,Zhen-Xing Xiong,Wen-Yue Mei,Jiang-Feng Ying,Guo-Qing |
dc.subject.por.fl_str_mv |
DEAE cellulose Nuclease p1 Immobilization Characterization |
topic |
DEAE cellulose Nuclease p1 Immobilization Characterization |
description |
Effects of various factors, such as pH, ionic strength, glutaraldehyde concentration, enzyme amount and immobilization time, on enzyme activity were investigated. The immobilization conditions were optimized by orthogonal experiments. Characterizations of immobilized nuclease p1 were also evaluated. Through orthogonal optimization, the optimal immobilization conditions were as follows: pH 5.6, ionic strength 0.125, glutaraldehyde concentration 0.20% and immobilization time 2.0 h. Optimal pH of immobilized enzyme was 5.8. Optimal temperature of immobilized enzyme was 70ºC. Thermal, operational and storage stabilities of the enzyme were improved after it was immobilized on DEAE cellulose. Michaelis constant Km of immobilized enzyme at 69ºC was found to be 27.21 g/l by the Lineweaver-Burk plot. |
publishDate |
2010 |
dc.date.none.fl_str_mv |
2010-03-01 |
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=S0104-66322010000100003 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322010000100003 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0104-66322010000100003 |
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 |
Brazilian Society of Chemical Engineering |
publisher.none.fl_str_mv |
Brazilian Society of Chemical Engineering |
dc.source.none.fl_str_mv |
Brazilian Journal of Chemical Engineering v.27 n.1 2010 reponame:Brazilian Journal of Chemical Engineering instname:Associação Brasileira de Engenharia Química (ABEQ) instacron:ABEQ |
instname_str |
Associação Brasileira de Engenharia Química (ABEQ) |
instacron_str |
ABEQ |
institution |
ABEQ |
reponame_str |
Brazilian Journal of Chemical Engineering |
collection |
Brazilian Journal of Chemical Engineering |
repository.name.fl_str_mv |
Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ) |
repository.mail.fl_str_mv |
rgiudici@usp.br||rgiudici@usp.br |
_version_ |
1754213173082193920 |