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090			_aB-19886
245	1	0	_aCultivation at 6-10 C is an effective strategy to overcome the insolubility of recombinant proteins in Escherichia coli
490	0		_vProtein expression and purification, 82(2), p.297-301, 2012
520	3		_aProtein expression in Escherichia coli at 15-25°C is widely used to increase the solubility of recombinant proteins. However, many recombinant proteins are insolubly expressed even at those low temperatures. Here, we show that recombinant proteins can be expressed as soluble forms by simply lowering temperature to 6-10°C without cold adapted chaperon systems. By using E. coli Rosetta-gami2(DE3), we obtained 1.8 and 0.9mg of Cryptopygus antarticus mannanase (CaMan)and cellulase (CaCel)from 1l culture grown at 6 and 10°C, respectively. Cultivation at 10°C also led to successful expression of EM3L7 (a lipase isolated from a metagenomic library)in a soluble form in E. coli BL21(DE3). Consequently, E. coli cultivation at 6-10°C is an effective strategy for overcoming a major hurdle of the inclusion body formation.
650	1	4	_aPROTEIN EXPRESSION
650	1	4	_aE. COLI
650	1	4	_aEXTREMELY LOW TEMPERATURE
700	1	2	_aSong, J. M.
700	1	2	_aAn, Y. J.
700	1	2	_aKang, M. H.
700	1	2	_aLee, Y. H.
700	1	2	_aCha, S. S.
856	4	0	_uhttps://drive.google.com/file/d/14VYn7JoWqJHay54p76fwt86tgSLKMWD_/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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