The pectinolytic enzyme of Selenomonas ruminantium |
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Authors: | Kvetoslava Heinrichova Maria Wojciechowicz A Ziolecki |
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Institution: | Institute of Chemistry, Slovak Academy of Sciences, 80933 Bratislava, Czechoslovakia;Institute of Animal Physiology and Nutrition, Polish Academy of Sciences, 05–110 Jablonna, Poland |
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Abstract: | 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°. The enzyme degraded polymeric substrates by hydrolysis of digalacturonic acid units from the non-reducing end; the best substrate was nona-galacturonic acid. Unsaturated trigalacturonate was also degraded, but 30% slower than the saturated analogue. The enzyme was classified as a poly (1,4-aP-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. |
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