The pectinolytic enzyme ofSelenomonas ruminantium
| Autor: | Maria Wojciechowicz, Kvetoslava Heinrichová, A. Ziolecki |
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| Rok vydání: | 1989 |
| Předmět: |
Rumen
Glycoside Hydrolases Polymers Applied Microbiology and Biotechnology Microbiology Substrate Specificity Gel permeation chromatography chemistry.chemical_compound Hydrolysis Animals Selenomonas ruminantium chemistry.chemical_classification Gram-Negative Anaerobic Bacteria biology Viscosity Temperature Substrate (chemistry) Hydrogen-Ion Concentration Chromatography Ion Exchange biology.organism_classification Enzyme assay Kinetics Polygalacturonase Monomer Enzyme Biochemistry chemistry Chromatography Gel biology.protein Pectins Cattle Bacteria |
| Zdroj: | Journal of Applied Bacteriology. 66:169-174 |
| ISSN: | 0021-8847 |
| DOI: | 10.1111/j.1365-2672.1989.tb02466.x |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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