Purification and Characterization of an Exo α-1, 2-Mannanase from Flavobacterium dormitator var. glucanolyticae

Abstract

An extremely purified preparation of an exo α-1, 2-mannanase (EC. 3. 2. 1. 24) has been obtained from the culture filtrate of Flavobacterium dormitator var. glucanolyticae by using yeast mannan as substrate. The molecular weight of the enzyme was estimated to be 900, 000. The enzyme showed pH optimum of 7.0 and was stable at pH 6.0. The Km value of the enzyme for yeast mannan was 0.16%. The enzyme did not seem to be Zn²⁺-dependent and was highly specific for α-1, 2-mannosidic bonds in yeast mannan.