Effects of Moranoline, 4-O-α-D-Glucopyranosylmoranoline and Their N-Substituted Derivatives on Thermostability of Cyclodextrin Glycosyltransferase, Glucoamylase, and β-Amylase

抄録

In repeated glycosylmoranolines synthetic reaction at 55°C, cyclodextrin glycosyltransferase (CGT-ase, EC 2.4.1.19) from Bacillus stearothermophilus retained its activity for more than 600 days. A main stabilizing compound was found to be 4-O-α-D-glucopyranosylmoranoline. The thermostabilizing activities of moranoline, 4-O-α-D-glucopyranosylmoranoline, and their N-substituted derivatives were studied. Moranoline and its N-substituted derivatives stabilized glucoamylase. 4-O-α-D-Glucopyranosylmoranoline and its N-substituted derivatives stabilized CGT-ase and β-amylase.