Purification and Properties of Inulinase from Arthrobacter globiformis S64—1

A bacterium, Arthrobacter globiformis S64—1, produced an inulinase in the culture broth. The enzyme was purified 442-fold by DEAE-Toyopearl chromatographies. It showed maximal activity at 40°C and pH 6.5. The enzyme activity was inhibited strongly by Hg²⁺, Fe³⁺, Cu²⁺ and EDTA. The molecular weight of the enzyme was estimated to be 100,000 by SDS-PAGE. The isoelctric point of the enzyme was estimated to be 4.8 by isoelectric focusing on a polyacrylamide gel. The enzyme degraded inulin through an exo-type reaction.