Purification and some properties of soybean saponin hydrolase from Aspergillus oryzae KO-2.

Article abstract of DOI:10.1080/00021369.1991.10870531

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 degrees C 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 degrees C. The Km and Vmax for soyasaponin I were 0.48 mM and 9.8 mumol/hr mg protein, respectively. After hydrolysis with the enzyme, soyasapogenol B and alpha-L-rhamnopyranosyl (1----2)-beta-D-galactopyranosyl (1----2)-D-glucuronopyranoside were released from soyasaponin I.

Full text of DOI:10.1080/00021369.1991.10870531

Agricultural and Biological Chemistry
ISSN: 0002-1369 (Print) (Online) Journal homepage: http://www.tandfonline.com/loi/tbbb19
Purification and Some Properties of Soybean
Saponin Hydrolase from Aspergillus oryzae KO-2
Shigemitsu Kudou, Iwao Tsuizaki, Teiji Uchida & Kazuyoshi Okubo
To cite this article: Shigemitsu Kudou, Iwao Tsuizaki, Teiji Uchida & Kazuyoshi Okubo (1991)
Purification and Some Properties of Soybean Saponin Hydrolase from Aspergillus oryzae KO-2,
Agricultural and Biological Chemistry, 55:1, 31-36, DOI: 10.1080/00021369.1991.10870531
To link to this article: http://dx.doi.org/10.1080/00021369.1991.10870531
Published online: 08 Sep 2014.
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Date: 10 June 2016, At: 15:10