Endo-polygalacturonate lyase of Cytophaga johnsonii

Sundarraj, Nirmala ; Bhat, J. V. (1971) Endo-polygalacturonate lyase of Cytophaga johnsonii Archives of Microbiology, 77 (2). pp. 155-164. ISSN 0302-8933

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Related URL: http://dx.doi.org/10.1007/BF00408608


An extracellular endopolygalacturonate lyase of Cytophaga johnsonii was purified from the culture filtrate. It appeared to be homogeneous as judged by polyacrylamide gel electrophoresis at pH 8.6 as well as pH 4.3. The purified enzyme had a pH optimum around 9.0 and required Ca++ ions for its maximum activity. The apparent Km for polygalacturonic acid was found to be 0.22%. Both paper and column chromatography indicated formation and accumulation of an unsaturated monomer along with unsaturated di-, tri-, tetra- and pentamers from polygalacturonic acid by the enzyme action, indicating that the enzyme cleaved the substrate randomly in a non-hydrolytic manner. The glycosidic linkage next to the non-reducing end of polygalacturonic acid was not resistant to attack by this enzyme unlike in other known polygalacturonate lyases.

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