High-Level Periplasmic Expression in Escherichia coli Using a Eukaryotic Signal Peptide: Importance of Codon Usage at the 5′ End of the Coding Sequence

2000 ◽  
Vol 20 (2) ◽  
pp. 252-264 ◽  
Author(s):  
David P. Humphreys ◽  
Mukesh Sehdev ◽  
Andrew P. Chapman ◽  
Ravindra Ganesh ◽  
Bryan J. Smith ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Codon Usage ◽  
Signal Peptide ◽  
Coding Sequence ◽  
Periplasmic Expression ◽  
Expression In Escherichia Coli ◽  
High Level

High-Level Expression in Escherichia coli, Purification and Kinetic Characterization of LAPTc, a Trypanosoma cruzi M17-Aminopeptidase

2019 ◽  
Vol 38 (2) ◽  
pp. 167-180 ◽  
Author(s):  
Maikel Izquierdo ◽  
Mirtha Elisa Aguado ◽  
Martin Zoltner ◽  
Jorge González-Bacerio
Keyword(s):  
Escherichia Coli ◽  
Trypanosoma Cruzi ◽  
Kinetic Characterization ◽  
High Level Expression ◽  
Expression In Escherichia Coli ◽  
High Level

scholarly journals Characterization and High-Level Periplasmic Expression of Thermostable α-Carbonic Anhydrase from Thermosulfurimonas Dismutans in Escherichia Coli for CO2 Capture and Utilization

2019 ◽  
Vol 21 (1) ◽  
pp. 103 ◽  
Author(s):  
Byung Hoon Jo ◽  
In Seong Hwang
Keyword(s):  
Escherichia Coli ◽  
Carbonic Anhydrase ◽  
Co2 Capture ◽  
Industrial Applications ◽  
Expression Level ◽  
High Level Expression ◽  
Whole Cell ◽  
Operational Conditions ◽  
Periplasmic Expression ◽  
High Level

Carbonic anhydrase (CA) is a diffusion-controlled enzyme that rapidly catalyzes carbon dioxide (CO2) hydration. CA has been considered as a powerful and green catalyst for bioinspired CO2 capture and utilization (CCU). For successful industrial applications, it is necessary to expand the pool of thermostable CAs to meet the stability requirement under various operational conditions. In addition, high-level expression of thermostable CA is desirable for the economical production of the enzyme. In this study, a thermostable CA (tdCA) of Thermosulfurimonas dismutans isolated from a deep-sea hydrothermal vent was expressed in Escherichia coli and characterized in terms of expression level, solubility, activity and stability. tdCA showed higher solubility, activity, and stability compared to those of CA from Thermovibrio ammonificans, one of the most thermostable CAs, under low-salt aqueous conditions. tdCA was engineered for high-level expression by the introduction of a point mutation and periplasmic expression via the Sec-dependent pathway. The combined strategy resulted in a variant showing at least an 8.3-fold higher expression level compared to that of wild-type tdCA. The E. coli cells with the periplasmic tdCA variant were also investigated as an ultra-efficient whole-cell biocatalyst. The engineered bacterium displayed an 11.9-fold higher activity compared to that of the recently reported system with a halophilic CA. Collectively these results demonstrate that the highly expressed periplasmic tdCA variant, either in an isolated form or within a whole-cell platform, is a promising biocatalyst with high activity and stability for CCU applications.

High-level expression in Escherichia coli of calcium-binding domains of an embryonic sea urchin protein

Gene ◽  
1984 ◽  
Vol 31 (1-3) ◽  
pp. 155-164 ◽  
Author(s):  
Mark Muesing ◽  
Clifford D. Carpenter ◽  
William H. Klein ◽  
Barry Polisky
Keyword(s):  
Escherichia Coli ◽  
Sea Urchin ◽  
Calcium Binding ◽  
High Level Expression ◽  
Expression In Escherichia Coli ◽  
Binding Domains ◽  
High Level

AGA/AGG codon usage in parasites: implications for gene expression in Escherichia coli

1995 ◽  
Vol 11 (9) ◽  
pp. 345-346 ◽  
Author(s):  
Jon R. Sayers ◽  
Helen P. Price ◽  
Padraic G. Fallon ◽  
Michael J. Doenhoff
Keyword(s):  
Gene Expression ◽  
Escherichia Coli ◽  
Codon Usage ◽  
Expression In Escherichia Coli
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