No abstract

A n exopolygalacturonate lyase (exo-PGL) was rapidly purified from the cells of E. carotovora subsp. carotovora with a modified cross-linked pectate (mdCLPA); the material CLPA waspartially degraded by an endopolygalacturonase to increase its adsorption capacity, followed by reduction with sodium borohydride. The Erwinia strain used here produced no pectolytic enzyme other than the exo-PGL under the present culture conditions. Since the mdCLPA was scarcely affected by the exo-PGL, the adsorbent can be repeatedly used for this enzyme purification with no risk of decomposition. The yield of the purified enzyme, which gave a single protein band on polyacrylamide gel electrophoresis, was about 43%. The apparent molecular weight was about 76,000. Exopolygalacturonate lyase (exo-PGL, EC 4.2.2.9) degrades the a-1,4 galacturonidic bonds in galacturonans and splits off 4,5unsaturated digalacturonic acid from the red ucing chain ends.1~3)