Transfructosylation Catalyzed by β-Fructofuranosidase I fromArthrobactersp. K-1

Transfructosylation of the β-fructofuranosidase I from Arthrobacter sp. K-1 was investigated. This enzyme catalyzed both transfructosylation and hydrolytic action, when it was incubated with sucrose alone. But in the presence of a suitable acceptor such as d-xylose and lactose, the enzyme catalyzed mostly transfructosylation and transferred the fructose residue preferentially to the acceptor. The enzyme had broad acceptor specificities. d-Xylose, d-galactose, l-sorbose, d- and l-fucose, d- and l-arabinose, maltose, isomaltose, cellobiose, lactose, melibiose, xylobiose, maltotriose, methyl β-glucoside, and galactoside were efficient acceptors in the transfructosylation. On the other hand, d-ribose, l-rhamnose, d-mannose, 2-deoxy-d-glucose, d-galactosamine, d-galacturonic acid, and 1-kestose were not efficient acceptors. Various primary alcohols, polyhydric alcohols including some sugar alcohols, and some glycosides acted as acceptors, but secondary alcohols with one hydroxyl group such as 2-propanol and 2-butanol were not effective as acceptors.