The pectinolytic enzyme of Selenomonas ruminantium.
A cell-bound pectinolytic enzyme was isolated from cells of Selenomonas ruminantium and purified about 360-fold. The optimum pH and temperature for enzyme activity was 7.0 and 40 degrees C. The enzyme degraded polymeric substrates by hydrolysis of digalacturonic acid units from the non-reducing end; the best substrate was nonagalacturonic acid. Unsaturated trigalacturonate was also degraded, but 30% slower than the saturated analogue. The enzyme was classified as a poly (1,4-alpha-D-galactosiduronate) digalacturono-hydrolase; EC 3.2.1.82. Another enzyme, hydrolysing digalacturonic acid to monomers, was also produced in a very small amount by this organism.
Heinrichova
K
K
Institute of Chemistry, Slovak Academy of Sciences, Bratislava, Czechoslovakia.
Wojciechowicz
M
M
Ziołecki
A
A
D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D006026:Glycoside Hydrolases / Q000302:isolation & purification*; D006089:Gram-Negative Anaerobic Bacteria / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010368:Pectins / Q000378:metabolism*; D011096:Polygalacturonase / Q000302:isolation & purification* / Q000378:metabolism; D011108:Polymers; D012417:Rumen / Q000382:microbiology*; D013379:Substrate Specificity; D013696:Temperature; D014783:Viscosity
D011108:Polymers; D010368:Pectins; D006026:Glycoside Hydrolases; D011096:Polygalacturonase; C003181:polygalacturonic acid