ArticleApplied and environmental microbiology1999
Enhancement of expression and apparent secretion of Erwinia chrysanthemi endoglucanase (encoded by celZ) in Escherichia coli B.
Article in Applied and environmental microbiology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 43 citations in OpenAlex.
- Extrapolation of design strategies for lignocellulosic biomass conversion to the challenge of plastic waste.Journal of industrial microbiology & biotechnology · 2022Article
- Innovations in CAZyme gene diversity and its modification for biorefinery applications.Biotechnology reports (Amsterdam, Netherlands) · 2020Review
- Developing Gram-negative bacteria for the secretion of heterologous proteins.Microbial cell factories · 2018Review
- Identification of a heterologous cellulase and its N-terminus that can guide recombinant proteins out of Escherichia coli.Microbial cell factories · 2015Article
- Challenges and advances in the heterologous expression of cellulolytic enzymes: a review.Biotechnology for biofuels · 2014Article
- Polysaccharide hydrolysis with engineered Escherichia coli for the production of biocommodities.Journal of industrial microbiology & biotechnology · 2013Review
- Cell surface display of a β-glucosidase employing the type V secretion system on ethanologenic Escherichia coli for the fermentation of cellobiose to ethanol.Journal of industrial microbiology & biotechnology · 2012Article
- Heterologous expression of plant cell wall degrading enzymes for effective production of cellulosic biofuels.Journal of biomedicine & biotechnology · 2012Review
- Engineering the Salmonella type III secretion system to export spider silk monomers.Molecular systems biology · 2009Article
- Microbial cellulose utilization: fundamentals and biotechnology.Microbiology and molecular biology reviews : MMBR · 2002Review
- Gene integration and expression and extracellular secretion of Erwinia chrysanthemi endoglucanase CelY (celY) and CelZ (celZ) in ethanologenic Klebsiella oxytoca P2.Applied and environmental microbiology · 2001Article
- Synergistic hydrolysis of carboxymethyl cellulose and acid-swollen cellulose by two endoglucanases (CelZ and CelY) from Erwinia chrysanthemi.Journal of bacteriology · 2000Article
- Improving health from the inside: Use of engineered intestinal microorganisms as in situ cytokine delivery system.BioengineeredArticle
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli B has been engineered as a biocatalyst for the conversion of lignocellulose into ethanol. Previous research has demonstrated that derivatives of E. coli B can produce high levels of Erwinia chrysanthemi endoglucanase (encoded by celZ) as a periplasmic product and that this enzyme can function with commercial fungal cellulase to increase ethanol production. In this study, we have demonstrated two methods that improve celZ expression in E. coli B. Initially, with a low-copy-number vector, two E. coli glycolytic gene promoters (gap and eno) were tested and found to be less effective than the original celZ promoter. By screening 18,000 random fragments of Zymomonas mobilis DNA, a surrogate promoter was identified which increased celZ expression up to sixfold. With this promoter, large polar inclusion bodies were clearly evident in the periplasmic space. Sequencing revealed that the most active surrogate promoter is derived from five Sau3A1 fragments, one of which was previously sequenced in Z. mobilis. Visual inspection indicated that this DNA fragment contains at least five putative promoter regions, two of which were confirmed by primer extension analysis. Addition of the out genes from E. chrysanthemi EC16 caused a further increase in the production of active enzyme and facilitated secretion or release of over half of the activity into the extracellular environment. With the most active construct, of a total of 13,000 IU of active enzyme per liter of culture, 7,800 IU was in the supernatant. The total active endoglucanase was estimated to represent 4 to 6% of cellular protein.
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