Skip to main content
SpringerLink
Log in

Endo-polygalacturonate lyase of Cytophaga johnsonii

  • Published:
Archiv für Mikrobiologie Aims and scope Submit manuscript

Summary

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 K mfor 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.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

Abbreviations

PG lyase:

Polygalacturonate lyase

Tris:

Tris (hydroxymethyl) aminomethane

References

  • Albersheim, P., Neukom, H., Deuel, H.: Splitting of pectin chain molecules in neutral solutions. Arch. Biochem. 90, 46–51 (1960a).

    PubMed  Google Scholar 

  • ———: Über die Bildung von ungesättigten Abbauprodukten durch ein pektinabbauendes Enzym. Helv. chim. Acta 43, 1422–1426 (1960b).

    Google Scholar 

  • Anderson, R. L., Ordal, E. J.: Cytophaga succinicans Sp. N., a facultatively anaerobic, aquatic myxobacterium. J. Bact. 81, 130–138 (1961).

    PubMed  Google Scholar 

  • Andrews, P.: Estimation of molecular weights of proteins by Sephadex gel-filtration. Biochem. J. 91, 222–233 (1964).

    Google Scholar 

  • Bacon, J. S. D., Edelman, J.: The carbohydrates of the Jerusalem Artichoke and other compositae. Biochem. J. 48, 114–126 (1951).

    Google Scholar 

  • Bhat, J. V., Jayasankar, N. P., Agate, A. D., Bilimoria, M. H.: Microbial degradation of pectic substances. Biochem. Rev. India 37, 23–29 (1966).

    Google Scholar 

  • Davis, B. J.: Disc electrophoresis. II. Method and application to human proteins. Ann. N. Y. Acad. Sci. 121, 404–427 (1964).

    PubMed  Google Scholar 

  • Edstrom, R. D., Phaff, H. J.: Eliminative cleavage of pectin and oligogalacturonide methyl esters by pectin trans-eliminase. J. biol. Chem. 239, 2409–2415 (1964).

    PubMed  Google Scholar 

  • French, D., Wild, G. M.: Correlation of carbohydrate structure with papergram mobility. J. Amer. chem. Soc. 75, 2612–2616 (1953).

    Google Scholar 

  • Fuchs, A.: The trans-eliminative breakdown of Na-polygalacturonate by Pseudomonas fluorescens. Antonie v. Leeuwenhoek 31, 323–340 (1965).

    Google Scholar 

  • Kamat, N. K., Bhat, J. V.: Pectin trans-eliminase activity in Cytophaga. Curr. Sci. 36, 486 (1967).

    Google Scholar 

  • Lanning, M. C., Cohen, S. S.: The detection and estimation of 2-ketohexonic acids. J. biol. Chem. 189, 109–114 (1951).

    PubMed  Google Scholar 

  • Lowry, O. H., Rosebrough, N. J., Farr, A. L., Randall, R. J.: Protein measurement with the folin phenol reagent. J. biol. Chem. 193, 265–275 (1951).

    PubMed  Google Scholar 

  • MacMillan, J. D., Vaughn, R. H.: Purification and properties of a polygalacturonic acid trans-eliminase produced by Clostridium multiferans. Biochemistry 3, 564–572 (1964).

    Google Scholar 

  • Moran, F., Nasuno, S., Starr, M. P.: Extracellular and intracellular polygalacturonic acid trans-eliminase of Erwinia caratovora. Arch. Biochem. 123, 298–306 (1968).

    PubMed  Google Scholar 

  • Nagel, C. W., Anderson, M. M.: Action of a bacterial trans-eliminase on normal and unsaturated oligogalacturonic acids. Arch. Biochem. 112, 322–330 (1965).

    Google Scholar 

  • —, Vaughn, R. H.: The characteristics of a polygalacturonase produced by Bacillus polymyxa. Arch. Biochem. 93, 344–352 (1961a).

    PubMed  Google Scholar 

  • ——: The degradation of oligogalacturonides by the polygalacturonase of Bacillus polymyxa. Arch. Biochem. 94, 328–332 (1961b).

    PubMed  Google Scholar 

  • Nasuno, S., Starr, M. P.: Polygalacturonic acid trans-eliminase of Xanthomonas campestris. Biochem. J. 104, 178–185 (1967).

    PubMed  Google Scholar 

  • Patel, D. S., Phaff, H. J.: On the mechanism of action of yeast endo-polygalacturonase on oligogalacturonides and their reduced and oxidised derivatives. J. biol. Chem. 234, 237–241 (1959).

    PubMed  Google Scholar 

  • Stanier, R. Y.: The Cytophaga group: A contribution to the biology of myxobacteria. Bact. Rev. 6, 143–196 (1942).

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Microbiology and Pharmacology Laboratory, Indian Institute of Science, Bangalore 12, India

    Nirmala Sundarraj & J. V. Bhat

Authors
  1. Nirmala Sundarraj
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. J. V. Bhat
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Sundarraj, N., Bhat, J.V. Endo-polygalacturonate lyase of Cytophaga johnsonii . Archiv. Mikrobiol. 77, 155–164 (1971). https://doi.org/10.1007/BF00408608

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00408608

Keywords

Search

Navigation