1887

Abstract

A poly(l,4-α--galacturonide) lyase (EC 4.2.2.2) from the culture fluid of was purified about 20-fold. The optimum pH and temperature for enzyme activity were 8·0 and 40C. The enzyme required Ca and was inhibited by EDTA; it preferred polygalacturonate as substrate, cleaving 1,4-α-glycosidic linkages randomly to form unsaturated galacturonates, mainly the unsaturated digalacturonate. Some properties of the crude and purified enzyme preparations are described. An exopolygalacturonase is also produced by this organism.

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1980-03-01
2022-01-20
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