Abstract
The activity of soluble cyclodextrin glycosyltransferase was increased by 40% without formation of inclusion bodies by induction at low temperature with the addition of 10 mM CaCl2 into the medium, when the corresponding gene was expressed in two recombinant E. coli. Furthermore, the protein expressed at 25 °C had approximately 30% higher specific activity than that expressed at 30 °C. The two different hosts, promoters, and media showed the same result, indicating that this simple method can be used in expressing other proteins.
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