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Expolygalacturonase from Suspension Cultures of Marchantia polymorpha1: Its Presence and Involvement in Pectic Polysaccharide Degradation

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  • Biology
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Abstract

Polygalacturonase was isolated from cell suspension cultures of a thalloid liverwort, Marchantia polymorpha. The enzyme in the `buffer-soluble' protein fraction was dialyzed at pH 5.2 and further purified 91-fold by a combination of chromatographic techniques including CM-Sephadex, Sephacryl S-200, DEAE-Sephadex, and Sephadex G-200. The purified enzyme had an optimum activity in the pH range at 3.6 to 3.8 and molecular weight of 76,000 daltons, and its activity was not stimulated by cations. The enzyme was identified as an exohydrolase from viscometric data and chromatographic analysis of the reaction products.

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