Engineering of factors determining alpha-amylase and cyclodextrin glycosyltransferase specificity in the cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1.

Characterization of the F196G mutant CGTase of T. thermosulfurigenes EM1 revealed that cyclization, coupling and disproportionation activities had become drastically reduced in the mutant F 196G(delta'DE), but its saccharifying activity had doubled, reaching the highest level ever reported for a CGT enzyme.