A polygalacturonate lyase produced by Lachnospira multiparus isolated from the bovine rumen.
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.
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002417:Cattle; D006089:Gram-Negative Anaerobic Bacteria / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D010368:Pectins; D011133:Polysaccharide-Lyases / Q000302:isolation & purification / Q000378:metabolism*; D012417:Rumen / Q000382:microbiology; D013696:Temperature
D010368:Pectins; D011133:Polysaccharide-Lyases; C023911:pectate lyase; D002118:Calcium