Neopullulanase Exhibits Distinct Specificity toward Amylose and Amylopectin

概要

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Neopullulanase was the key enzyme to open the door for the formulation of the concept of the aamylasefamily. The enzyme catalyzes both hydrolysis and transglycosylation at α-1, 4- and α-1, 6-glucosidic linkages through one active center. We found a unique macromolecule recognition by the enzyme. A mixture of amylose and amylopectin from various sources was used as the substrate. Neopullulanase completely hydrolyzedamylose to maltose and a small amount of glucose, but scarcely hydrolyzed amylopectin. Although the molecular mass of potato amylopectin (approximately 10<SUP>8</SUP> Da) decreased slightly, the degradation of amylopectincompletely halted at the molecular mass of approximately 10<SUP>7</SUP>Da. This difference in action on two macromolecules was also found in cyclomaltodextrinase and maltogenic amylase from Bacillus licheniformis.
日本応用糖質科学会の論文
2003-07-14