Studies on the Enzymes Acting on Araban

Abstract

Arabanase was purified by various procedures of gel filtrations and column chromatographies from the submerged culture filtrate of Aspergillus niger grown on the medium containing beet-araban as a carbon source, and the properties of the enzyme was examined. The purified enzyme was homogeneous protein in ultracentrifugal analysis, the optimum pH for enzymatic action was 4.0. The enzyme was thermostable at pH 6.0, namely, even after heating at 98°C for 10 minutes, 20.8 per cent of the initial activity still remained. The enzyme hydrolyzed beet-araban with producing l-arabinose.