Purification and Some Properties of Soybean Saponin Hydrolase from Aspergillus oryzae KO-2(Biological Chemistry)

概要

論文の詳細を見る
We had investigated the enzymatic hydrolysis of soybean saponins and selected soybean saponin hydrolase from Aspergillus oryzae KO-2. We attempted purification of this enzyme for further characterization. This enzyme was purified 1500-fold using ammonium sulfate fractionation and Sephadex G-200 gel filtrations. The enzyme was electrophoretically homogeneous and a glycoprotein by PAS staining. By gel filtration, the molecular weight of enzyme was 158,000 and SDS-PAGE showed the enzyme to have a tetrameric structure composed of heterogeneous subunits of 35,000 and 45,000. The enzyme activity was stable at temperatures below 40℃ and stable from pH 5.0 to 8.0. The optimum pH was pH 4.5 to 5.0 and the optimum temperature was 50℃. The Km and V_<max> for soyasaponin I were 0.48 m_M and 9.8 μmol/hr mg protein, respectively. After hydrolysis with the enzyme, soyasapogenol B and α-L-rhamnopyranosyl (1→2)-β-D-galactopyranosyl (1→2)-D-glucuronopyranoside were released from soyasaponin I.
社団法人日本農芸化学会の論文
1991-01-23