Change in compactness of inclusion bodies of recombinant β-galactosidase expressed in the <Emphasis Type="Italic">araBAD</Emphasis> promoter system of <Emphasis Type="Italic">Escherichia coli</Emphasis> |
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Authors: | Ji-Hyeon Yeon Kyung-Hwan Jung |
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Institution: | (1) Division of Food and Biotechnology, Chungju National University, Jeungpyung-Gun, Chungbuk, 368-701, South Korea;(2) BK21-NURI Committee, Korea Research Foundation, Yangjae-Dong, Seocho-Gu, Seoul, 137-943, Korea |
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Abstract: | 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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Keywords: | |
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