Shigetaka Okada

TL;DR: Analysis of the products indicated that the enzyme catalyzes an intramolecular transglycosylation reaction on amylose to produce cyclic α-1,4-glucan (cycloamylose), and confirmation of the cyclic structure was achieved by demonstrating the absence of reducing and nonreducing ends, resistance to hydrolysis by glucoamylase, and by “time of flight” mass spectrometry.

TL;DR: The crystal structure of a hydrated cycloamylose containing 26 glucose residues (cyclomaltohexaicosaose, CA26), which has been determined by real/reciprocal space recycling starting from randomly positioned atoms or from an oriented diglucose fragment, provides conclusive evidence for the structure of V-amylOSE.

TL;DR: A new model for the action of CGTase on amylose was proposed, which may contradict the widely held view of the cyclization reaction of C GTase, and produced large cyclic α-1,4-glucans except that the final major product was α-CD.

TL;DR: A detailed analysis of the activity of T. aquaticus ATCC 33923 amylomaltase with maltooligosaccharides indicated that the catalytic properties of this enzyme differ from those of E. coliamylmaltase and the plant D-enzyme.

TL;DR: In this paper, linear or branched glucan was produced from glucose-1-phosphate by glucan phosphorylase alone or together with bracnhing enzyme.