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KMID : 1094720100150040620
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Biotechnology and Bioprocess Engineering
2010 Volume.15 No. 4 p.620 ~ p.625
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Change in compactness of inclusion bodies of recombinant β-galactosidase expressed in the araBAD promoter system of Escherichia coli
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Yeon Ji-Hyeon
Jung Kyung-Hwan
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Abstract
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We investigated the relevance of the relationship between the compactness of β-galactosidase inclusion bodies (β-gal IBs) and their enhanced enzymatic activity with or without the addition of D-fucose (inducer analog) or methyl α-D-glucopyranoside (α-MG, catabolite repressor) after induction in the araBAD promoter system of Escherichia coli. Experiments conducted to evaluate the solubilization of β-gal IBs in guanidine hydrochloride as well as their trypsin degradation and temperature stability revealed that β-gal IBs expressed in response to the addition of D-fucose or α-MG had a looser structure. Additionally, β-gal IBs expressed when D-fucose or α-MG was added were more quickly solubilized in guanidine hydrochloride or degraded by trypsin-treatment than those produced when these compounds were not added. Moreover, the activity of β-gal IBs expressed when D-fucose or α-MG were added was less stable at various temperatures. Consequently, we deduced that the looser structure of β-gal IBs resulted in enhanced enzymatic activity of β-gal IBs upon addition of D-fucose or α-MG after induction.
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KEYWORD
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araBAD promoter of Escherichia coli, compactness of inclusion body, D-fucose, inclusion body of β-galactosidase, methyl α-D-glucopyranoside
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