Enhancement of Escherichia coli cellulolytic activity by co-production of beta-glucosidase and endoglucanase enzymes

Cellulase is a group of enzymes (endoglucanase, exoglucanase and beta-glucosidase) required for cellulosic feedstock hydrolysis during bioethanol production. The use of recombinant cellulase is a strategy to reduce the enzyme cost. In this context, the present work describes the construction of a ce...

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Autores principales:	Rodrigues,André L, Cavalett,Angélica, Lima,André O.S
Lenguaje:	English
Publicado:	Pontificia Universidad Católica de Valparaíso 2010
Materias:	beta-glucosidase cellulase cassette cellulose bioconversion endoglucanase heterologous expression
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582010000500005
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spelling	oai:scielo:S0717-345820100005000052011-05-24Enhancement of Escherichia coli cellulolytic activity by co-production of beta-glucosidase and endoglucanase enzymesRodrigues,André LCavalett,AngélicaLima,André O.S beta-glucosidase cellulase cassette cellulose bioconversion endoglucanase heterologous expression Cellulase is a group of enzymes (endoglucanase, exoglucanase and beta-glucosidase) required for cellulosic feedstock hydrolysis during bioethanol production. The use of recombinant cellulase is a strategy to reduce the enzyme cost. In this context, the present work describes the construction of a cellulase expression vector (pEglABglA), which allowed constitutive co-expression of endoglucanase A (EglA) from an endophytic Bacillus pumilus and the hyperthermophilic β-glucosidase A (BglA) from Fervidobacterium sp. in Escherichia coli. When compared to the non-modified strain DH5α, the recombinant Escherichia coli DH5α (pEglABglA) reduced fivefold the viscosity of the carboxymethylcellulose medium (CMC-M). Also, it presented almost 30-fold increase in reducing sugar released from CMC-M, enabling the recombinant strain to grow using CMC as the sole carbon and energy source. When cultivated in rich media, specific growth rates of recombinant E. coli strains BL21, JM101 and Top10 were higher than those of DH5α and DH10B strains. The constructed plasmid (pEglABglA) can be used as backbone for further cellulase gene addition, which may enhance even more E. coli cellulolytic capacity and growth rate.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.13 n.5 20102010-09-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582010000500005en
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	beta-glucosidase cellulase cassette cellulose bioconversion endoglucanase heterologous expression
spellingShingle	beta-glucosidase cellulase cassette cellulose bioconversion endoglucanase heterologous expression Rodrigues,André L Cavalett,Angélica Lima,André O.S Enhancement of Escherichia coli cellulolytic activity by co-production of beta-glucosidase and endoglucanase enzymes
description	Cellulase is a group of enzymes (endoglucanase, exoglucanase and beta-glucosidase) required for cellulosic feedstock hydrolysis during bioethanol production. The use of recombinant cellulase is a strategy to reduce the enzyme cost. In this context, the present work describes the construction of a cellulase expression vector (pEglABglA), which allowed constitutive co-expression of endoglucanase A (EglA) from an endophytic Bacillus pumilus and the hyperthermophilic β-glucosidase A (BglA) from Fervidobacterium sp. in Escherichia coli. When compared to the non-modified strain DH5α, the recombinant Escherichia coli DH5α (pEglABglA) reduced fivefold the viscosity of the carboxymethylcellulose medium (CMC-M). Also, it presented almost 30-fold increase in reducing sugar released from CMC-M, enabling the recombinant strain to grow using CMC as the sole carbon and energy source. When cultivated in rich media, specific growth rates of recombinant E. coli strains BL21, JM101 and Top10 were higher than those of DH5α and DH10B strains. The constructed plasmid (pEglABglA) can be used as backbone for further cellulase gene addition, which may enhance even more E. coli cellulolytic capacity and growth rate.
author	Rodrigues,André L Cavalett,Angélica Lima,André O.S
author_facet	Rodrigues,André L Cavalett,Angélica Lima,André O.S
author_sort	Rodrigues,André L
title	Enhancement of Escherichia coli cellulolytic activity by co-production of beta-glucosidase and endoglucanase enzymes
title_short	Enhancement of Escherichia coli cellulolytic activity by co-production of beta-glucosidase and endoglucanase enzymes
title_full	Enhancement of Escherichia coli cellulolytic activity by co-production of beta-glucosidase and endoglucanase enzymes
title_fullStr	Enhancement of Escherichia coli cellulolytic activity by co-production of beta-glucosidase and endoglucanase enzymes
title_full_unstemmed	Enhancement of Escherichia coli cellulolytic activity by co-production of beta-glucosidase and endoglucanase enzymes
title_sort	enhancement of escherichia coli cellulolytic activity by co-production of beta-glucosidase and endoglucanase enzymes
publisher	Pontificia Universidad Católica de Valparaíso
publishDate	2010
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582010000500005
work_keys_str_mv	AT rodriguesandrel enhancementofescherichiacolicellulolyticactivitybycoproductionofbetaglucosidaseandendoglucanaseenzymes AT cavalettangelica enhancementofescherichiacolicellulolyticactivitybycoproductionofbetaglucosidaseandendoglucanaseenzymes AT limaandreos enhancementofescherichiacolicellulolyticactivitybycoproductionofbetaglucosidaseandendoglucanaseenzymes
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Enhancement of Escherichia coli cellulolytic activity by co-production of beta-glucosidase and endoglucanase enzymes

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