A simple method to express soluble, highly active cyclodextrin glycosyltransferase in recombinant E-coli

The activity of soluble cyclodextrin glycosyltransferase was increased by 4 0% without formation of inclusion bodies by induction at low temperature wi th the addition of 10 mM CaCl2 into the medium, when the corresponding gene was expressed in two recombinant E. coli. Furthermore, the protein express ed at 25 degrees C had approximately 30% higher specific activity than that expressed at 30 degrees C. The two different hosts, promoters, and media s howed the same result, indicating that this simple method can be used in ex pressing other proteins.