SUMMARY: A polygalacturonase has been purified from the culture fluid of a strain of . The purified preparation was homogeneous when examined by ultracentrifugation. The hydrolysis of di- and trigalacturonic acids by the enzyme was undetectable. Tetragalacturonic acid was hydrolysed to tri- and monogalacturonic acids, while pentagalacturonic acid was hydrolysed to either tri- and digalacturonic acids or tetra- and monogalacturonic acids. The rate of hydrolysis of pentagalacturonic acid to tri- and digalacturonic acids was about four times as fast as that to tetra- and monogalacturonic acids. It was concluded that the enzyme can hydrolyse any glycosidic bond between the reducing end and the third galacturonic-acid unit from the non-reducing end of poly-galacturonic acid. The manner of hydrolysis of polygalacturonic acid by the enzyme is different from that of any other polygalacturonase reported so far.


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