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Summary: A poly(l,4-α-d-galacturonide) lyase (EC 4.2.2.2) from the culture fluid of Lachnospira multiparus was purified about 20-fold. The optimum pH and temperature for enzyme activity were 8·0 and 40°C. The enzyme required Ca2+ 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.