Roles of Heat-Shock Chaperones in the Production of Recombinant Proteins in Escherichia coli

2004 ◽  
pp. 143-161 ◽  
Author(s):  
Frank Hoffmann ◽  
Ursula Rinas
Keyword(s):  
Escherichia Coli ◽  
Heat Shock ◽  
Recombinant Proteins

Expression and characterization of an α-glucosidase from Thermoanaerobacter ethanolicus JW200 with potential for industrial application

Biologia ◽  
2009 ◽  
Vol 64 (6) ◽  
Author(s):  
Yue-Hong Wang ◽  
Yu Jiang ◽  
Zuo-Ying Duan ◽  
Wei-Lan Shao ◽  
Hua-Zhong Li
Keyword(s):  
Escherichia Coli ◽  
Heat Shock ◽  
Optimal Condition ◽  
Industrial Application ◽  
Conversion Rate ◽  
Hydrolytic Activity ◽  
Thermoanaerobacter Ethanolicus ◽  
Transglycosylation Activity

AbstractIn this study, a new α-glucosidase gene from Thermoanaerobacter ethanolicus JW200 was cloned and expressed in Escherichia coli by a novel heat-shock vector pHsh. The recombinant α-glucosidase exhibited its maximum hydrolytic activity at 70°C and pH 5.0∼5.5. With p-nitrophenyl-α-D-glucoside as a substrate and under the optimal condition (70°C, pH 5.5), K m and V max of the enzyme was 1.72 mM and 39 U/mg, respectively. The purified α-glucosidase could hydrolyze oligosaccharides with both α-1,4 and α-1,6 linkages. The enzyme also had strong transglycosylation activity when maltose was used as sugar donor. The transglucosylation products towards maltose are isomaltose, maltotriose, panose, isomaltotriose and tetrasaccharides. The enzyme could convert 400 g/L maltose to oligosaccharides with a conversion rate of 52%, and 83% of the oligosaccharides formed were prebiotic isomaltooligosaccharides (containing isomaltose, panose and isomaltotriose).

scholarly journals Sequence of the lon gene in Escherichia coli. A heat-shock gene which encodes the ATP-dependent protease La.

1988 ◽  
Vol 263 (24) ◽  
pp. 11718-11728 ◽  
Author(s):  
D T Chin ◽  
S A Goff ◽  
T Webster ◽  
T Smith ◽  
A L Goldberg
Keyword(s):  
Escherichia Coli ◽  
Heat Shock ◽  
Heat Shock Gene ◽  
Shock Gene

Modulation of the Escherichia coli σ E (RpoE) heat‐shock transcription‐factor activity by the RseA, RseB and RseC proteins

1997 ◽  
Vol 24 (2) ◽  
pp. 355-371 ◽  
Author(s):  
Dominique Missiakas ◽  
Matthias P. Mayer ◽  
Marc Lemaire ◽  
Costa Georgopoulos ◽  
Satish Raina
Keyword(s):  
Escherichia Coli ◽  
Transcription Factor ◽  
Heat Shock ◽  
Heat Shock Transcription Factor ◽  
Transcription Factor Activity ◽  
Factor Activity

The solubility of recombinant proteins expressed in Escherichia coli is increased by otsA and otsB co-transformation

2007 ◽  
Vol 355 (1) ◽  
pp. 234-239 ◽  
Author(s):  
Tina Schultz ◽  
Jing Liu ◽  
Paola Capasso ◽  
Ario de Marco
Keyword(s):  
Escherichia Coli ◽  
Recombinant Proteins

scholarly journals The Functional Quality of Soluble Recombinant Polypeptides Produced in Escherichia coli Is Defined by a Wide Conformational Spectrum

2008 ◽  
Vol 74 (23) ◽  
pp. 7431-7433 ◽  
Author(s):  
Mónica Martínez-Alonso ◽  
Nuria González-Montalbán ◽  
Elena García-Fruitós ◽  
Antonio Villaverde
Keyword(s):  
Escherichia Coli ◽  
Green Fluorescent Protein ◽  
Recombinant Proteins ◽  
Fluorescent Protein ◽  
Native Structure ◽  
Functional Quality ◽  
Soluble Aggregates ◽  
Recombinant Polypeptides ◽  
Green Fluorescent

ABSTRACT We have observed that a soluble recombinant green fluorescent protein produced in Escherichia coli occurs in a wide conformational spectrum. This results in differently fluorescent protein fractions in which morphologically diverse soluble aggregates abound. Therefore, the functional quality of soluble versions of aggregation-prone recombinant proteins is defined statistically rather than by the prevalence of a canonical native structure.

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