Abstract
By using the highly purified cyclodextrin glucanotransferase ([EC. 2. 4. 1. 19], CGT-ase) from Bacillus stearothermophilus TC-60, intramolecular and intermolecular transglycosylation, hydrol ytic reaction on starch and α-, β- and γ-CD and disproportionation reaction on maltotriose were investigated to compare with those of CGT-ases from B. megaterium, B. circulans ATCC 9995 and B. macerans IFO 3490. CGT-ase from B, stearothermophilus was found to be a novel type of CGT-ase, different from CGT-ases of B. megaterium, B. circulans and B. macerans.
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