Purification and Some Properties of a New Levanase from Bacillus sp. No. 71

Abstract

A levanase from Bacillus sp. was purified to a homogeneous state. The enzyme had a molecular weight of 135, 000 and an isoelectric point of pH 4.7. The enzyme was most active at pH 6.0 and 40°C, stable from pH 6.0 to 10.0 for 20hr of incubation at 4°C and up to 30°C for 30 min of incubation at pH 6.0. The enzyme activity was inhibited by Ag⁺, Hg²⁺, Cu²⁺, Fe³⁺, Pb²⁺, and p-chloromercuribenzoic acid. The enzyme hydrolyzed levan and phlein endowise to produce levanheptaose as a main product. The limit of hydrolysis of levan and phlein were 71% and 96%, respectively.