Characterization of a cellulose binding domain from Clostridium cellulovorans endoglucanase-xylanase D and its use as a fusion partner for soluble protein expression in Escherichia coli.

Abstract

Different chimeric proteins combining the non-catalytic C-terminal putative cellulose binding domain of Clostridium cellulovorans endoglucanase-xylanase D (EngD) with its proline-threonine rich region PT-linker, PTCBD(EngD), cellulose binding domain of C. cellulovorans cellulose binding protein A, CBD(CbpA), cohesin domains Cip7, Coh6 and CipC1 from… (More)
DOI: 10.1016/j.jbiotec.2008.05.004

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Cite this paper

@article{Xu2008CharacterizationOA, title={Characterization of a cellulose binding domain from Clostridium cellulovorans endoglucanase-xylanase D and its use as a fusion partner for soluble protein expression in Escherichia coli.}, author={Yin Xu and Frances C. Foong}, journal={Journal of biotechnology}, year={2008}, volume={135 4}, pages={319-25} }