| Literature DB >> 7391818 |
M Wojciechowicz, K Heinrichova, A Ziołecki.
Abstract
A poly(1,4-alpha-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 degrees C. The enzyme required Ca2+ and was inhibited by EDTA; it preferred polygalacturonate as substrate, cleaving 1,4-alpha-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.Entities:
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Year: 1980 PMID： 7391818 DOI： 10.1099/00221287-117-1-193
Source DB: PubMed Journal: J Gen Microbiol ISSN： 0022-1287