Host: Japan Agency for Marine-Earth Science and Technology
Co-host: Toyo University, Japan Society for the Promotion of Science
Pages 50-57
Neopullulanase catalyzes the hydrolysis of α-1,4- and α-1,6-glucosidic linkages, as well as transglycosylation to form α-1,4- and α-1,6-glucosidic linkages. Based on the series of experimental results using the neopullulanase, we pointed out the same catalytic machinery and the common catalytic mechanism of the enzymes that catalyze these four reactions, and thus, proposed and defined the concept of the α-amylase family. Mutational and structural analyses provided the conclusive proof that one active center of neopullulanase participate in all four reactions. We have been trying to interconvert glucanohydrolases/glucanotransferases, and their specificities and create tailor-made industrially useful enzymes based on the concept of the α-amylase family. We engineered Thermus amylomaltase to essentially erase hydrolytic activity and created perfect 4-α-glucanotransferase for the industrial production of cycloamylose.