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The pectinolytic enzyme of Selenomonas ruminantium
Author(s) -
Heinrichova Kvetoslava,
Wojciechowicz Maria,
Ziolecki A.
Publication year - 1989
Publication title -
journal of applied bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 0021-8847
DOI - 10.1111/j.1365-2672.1989.tb02466.x
Subject(s) - enzyme , substrate (aquarium) , biochemistry , chemistry , hydrolysis , hydrolase , bacteria , enzyme assay , monomer , microbiology and biotechnology , biology , organic chemistry , genetics , polymer , ecology
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.