Enhancement of escherichia coli cellulolytic activity by co-production of beta-glucosidase and endoglucanase enzymes
Electron. j. biotechnol
; 13(5): 5-6, Sept. 2010. ilus, tab
Article
in English
| LILACS
| ID: lil-591887
Responsible library:
CL1.1
ABSTRACT
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 beta-glucosidase A (BglA) from Fervidobacterium sp. in Escherichia coli. When compared to the non-modified strain DH5 alpha, the recombinant Escherichia coli DH5 alpha (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 DH5 alpha 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.
Full text:
Available
Collection:
International databases
Health context:
Neglected Diseases
Health problem:
Neglected Diseases
/
Zoonoses
Database:
LILACS
Main subject:
Cellulases
/
Escherichia coli
Language:
English
Journal:
Electron. j. biotechnol
Journal subject:
Biotechnology
Year:
2010
Document type:
Article
/
Project document
Affiliation country:
Brazil
Institution/Affiliation country:
Universidade do Vale do Itajaí/BR