1887

Abstract

Summary: 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 40°C. 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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/content/journal/micro/10.1099/00221287-117-1-193
1980-03-01
2019-10-22
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-117-1-193
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