An endo β-1, 6-glucanase (β-1, 6-glucan glucanohydrolase, E. C. 3. 2. 1.) has been purified from the culture filtrate of a strain resembling Rhizopus chinensis in homogeneous form. The procedures involved ammonium sulfate fractionation followed by column chromatography of DEAE-cellulose, CM-Sephadex C-50 and BioGel P-60.
Various physicochemical and chemical characteristics of the enzyme have been made clear, including complete amino acid composition. Optimum pH, optimum temperature, apparent activation energy for activity, Km and V_max are 5.5_??_6.0, 60°C, 4.39 Cal per mole, 9.39×10^-3_M glucose equivalents (0.169%) and 43.13 International Units, respectively. The enzyme required no metal ions for its activity, and it hydrolyzed β-1, 6-glucan larger than gentiotetraose, forming gentiobiose and gentiotriose as main products.

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