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Endo-polygalacturonate lyase of Cytophaga johnsonii

Sundarraj, Nirmala and Bhat, JV (1971) Endo-polygalacturonate lyase of Cytophaga johnsonii. In: Archiv für Mikrobiologie, 77 (2). pp. 155-164.

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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 Kmfor 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.

Item Type: Journal Article
Publication: Archiv für Mikrobiologie
Publisher: Springer Berlin
Additional Information: Copyright of this article belongs to Springer Berlin.
Department/Centre: Division of Biological Sciences > Microbiology & Cell Biology
Date Deposited: 16 Jun 2010 08:58
Last Modified: 23 Oct 2018 10:53
URI: http://eprints.iisc.ac.in/id/eprint/28457

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