Optimization of Endoglucanase Production from a Novel Bacterial Isolate, Arthrobacter sp. HPG166 and Characterization of Its Properties

Detalhes bibliográficos
Autor(a) principal: Huang,Shengwei
Data de Publicação: 2015
Outros Autores: Deng,Guanjun, Yang,Ying, Wu,Zhengyan, Wu,Lifang
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=S1516-89132015000500692
Resumo: ABSTRACTIn this study, a potential novel cellulolytic bacteriumArthrobacter sp. HPG166 was isolated from the hindgut of root-feeding larvaeHolotrichia parallela. Optimization of fermentation factors for endoglucanase production byArthrobacter sp. HPG166 was carried out via response surface methodology. Sodium carboxymethylcellulose 1.19% (w/v) and beef extract 0.35% (w/v) were the ideal combination of carbon and nitrogen sources for enzyme production; the optimum temperature and pH for cellulase production were 34°C and pH 8.0 respectively. Under the optimized fermentation conditions, the maximum endoglucanase activity of 1.411 U mL-1 was obtained. The crude endoglucanase was thermotolerant as it retained 50.31% of its activity after incubation at 70°C for an hour. Metal profile of the enzyme indicated that Mg2+ and Na+ were strong stimulators while Mn2+ and Co+ drastically inhibited its activity. Due to its particular characteristics, this enzyme could have potential for industrial applications.
id TECPAR-1_3481d3158f34dd0972c8962d6be372af
oai_identifier_str oai:scielo:S1516-89132015000500692
network_acronym_str TECPAR-1
network_name_str Brazilian Archives of Biology and Technology
repository_id_str
spelling Optimization of Endoglucanase Production from a Novel Bacterial Isolate, Arthrobacter sp. HPG166 and Characterization of Its PropertiesScarab larvaeCellulolytic bacteriaResponse surface methodologyThermotolerant cellulasesEffects of Metal ionsABSTRACTIn this study, a potential novel cellulolytic bacteriumArthrobacter sp. HPG166 was isolated from the hindgut of root-feeding larvaeHolotrichia parallela. Optimization of fermentation factors for endoglucanase production byArthrobacter sp. HPG166 was carried out via response surface methodology. Sodium carboxymethylcellulose 1.19% (w/v) and beef extract 0.35% (w/v) were the ideal combination of carbon and nitrogen sources for enzyme production; the optimum temperature and pH for cellulase production were 34°C and pH 8.0 respectively. Under the optimized fermentation conditions, the maximum endoglucanase activity of 1.411 U mL-1 was obtained. The crude endoglucanase was thermotolerant as it retained 50.31% of its activity after incubation at 70°C for an hour. Metal profile of the enzyme indicated that Mg2+ and Na+ were strong stimulators while Mn2+ and Co+ drastically inhibited its activity. Due to its particular characteristics, this enzyme could have potential for industrial applications.Instituto de Tecnologia do Paraná - Tecpar2015-10-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000500692Brazilian Archives of Biology and Technology v.58 n.5 2015reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/S1516-89132015050256info:eu-repo/semantics/openAccessHuang,ShengweiDeng,GuanjunYang,YingWu,ZhengyanWu,Lifangeng2015-11-06T00:00:00Zoai:scielo:S1516-89132015000500692Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2015-11-06T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false
dc.title.none.fl_str_mv Optimization of Endoglucanase Production from a Novel Bacterial Isolate, Arthrobacter sp. HPG166 and Characterization of Its Properties
title Optimization of Endoglucanase Production from a Novel Bacterial Isolate, Arthrobacter sp. HPG166 and Characterization of Its Properties
spellingShingle Optimization of Endoglucanase Production from a Novel Bacterial Isolate, Arthrobacter sp. HPG166 and Characterization of Its Properties
Huang,Shengwei
Scarab larvae
Cellulolytic bacteria
Response surface methodology
Thermotolerant cellulases
Effects of Metal ions
title_short Optimization of Endoglucanase Production from a Novel Bacterial Isolate, Arthrobacter sp. HPG166 and Characterization of Its Properties
title_full Optimization of Endoglucanase Production from a Novel Bacterial Isolate, Arthrobacter sp. HPG166 and Characterization of Its Properties
title_fullStr Optimization of Endoglucanase Production from a Novel Bacterial Isolate, Arthrobacter sp. HPG166 and Characterization of Its Properties
title_full_unstemmed Optimization of Endoglucanase Production from a Novel Bacterial Isolate, Arthrobacter sp. HPG166 and Characterization of Its Properties
title_sort Optimization of Endoglucanase Production from a Novel Bacterial Isolate, Arthrobacter sp. HPG166 and Characterization of Its Properties
author Huang,Shengwei
author_facet Huang,Shengwei
Deng,Guanjun
Yang,Ying
Wu,Zhengyan
Wu,Lifang
author_role author
author2 Deng,Guanjun
Yang,Ying
Wu,Zhengyan
Wu,Lifang
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Huang,Shengwei
Deng,Guanjun
Yang,Ying
Wu,Zhengyan
Wu,Lifang
dc.subject.por.fl_str_mv Scarab larvae
Cellulolytic bacteria
Response surface methodology
Thermotolerant cellulases
Effects of Metal ions
topic Scarab larvae
Cellulolytic bacteria
Response surface methodology
Thermotolerant cellulases
Effects of Metal ions
description ABSTRACTIn this study, a potential novel cellulolytic bacteriumArthrobacter sp. HPG166 was isolated from the hindgut of root-feeding larvaeHolotrichia parallela. Optimization of fermentation factors for endoglucanase production byArthrobacter sp. HPG166 was carried out via response surface methodology. Sodium carboxymethylcellulose 1.19% (w/v) and beef extract 0.35% (w/v) were the ideal combination of carbon and nitrogen sources for enzyme production; the optimum temperature and pH for cellulase production were 34°C and pH 8.0 respectively. Under the optimized fermentation conditions, the maximum endoglucanase activity of 1.411 U mL-1 was obtained. The crude endoglucanase was thermotolerant as it retained 50.31% of its activity after incubation at 70°C for an hour. Metal profile of the enzyme indicated that Mg2+ and Na+ were strong stimulators while Mn2+ and Co+ drastically inhibited its activity. Due to its particular characteristics, this enzyme could have potential for industrial applications.
publishDate 2015
dc.date.none.fl_str_mv 2015-10-01
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=S1516-89132015000500692
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000500692
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S1516-89132015050256
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.58 n.5 2015
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_ 1750318276959797248

Registros relacionados