Biotechnology Letters

, Volume 9, Issue 3, pp 219–224 | Cite as

Purification and properties of an endopolygalacturonase produced byRhizopusstolonifer

  • P. L. Manachini
  • M. G. Fortina
  • C. Parini


A polygalacturonase from culture filtrates of a strain ofRhizopusstolonifer was purified about 80 fold by ethanol precipitation, followed by ion exchange chromatography (CM-Sepharose 6B) and gel filtration (Sephadex G-100). The purified preparation was homogeneous when examined by PAGE. The enzyme is an endopolygalacturonase with an optimum catalytic activity at pH 5.0 and 45°C, and a molecular weight of 57,000±500 daltons. The activity was stimulated by Fe+++, Mg++, Co++, and inhibited by Mn++ and Zn++. The enzyme was stable in the pH range of 3.0 to 5.0. The purified enzyme was specific for nonmethoxylate polygalacturonic acid, with Km and Vmax values respectively of 0.19 mg/ml and 1.3 μmol/μg/min. In addition, this enzymatic preparation degraded pectic substances in organge peel.


Enzyme Precipitation Molecular Weight Chromatography Purification 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Andrews, P. (1964)Biochem. J. 91, 222–232Google Scholar
  2. Archer, S.A., and Fielding, A.H. (1979),J. Sci. Food Agric. 30, 711–723Google Scholar
  3. Baker, R.A., and Bruemmer, J.H. (1972)Agric. Food. Chem. 20, 1169–1173Google Scholar
  4. Barkai-Golan, R., Kopeliovitch, E., and Brady, C.J. (1986)Phytopat. 76, 42–45Google Scholar
  5. Bell, T.A., Etchells, J.L., and Jones, I.D. (1950)Food technol. 4, 157–163Google Scholar
  6. Cappellini, R.A. (1966)Phytopat. 56, 734–737Google Scholar
  7. Fogarty, W.M., and Kelly, C.T. (1983) Pectic enzymes. In:Microbial enzymes and biotechnology, W.M. Fogarty, ed., pp. 131–182, New York: Applied Science Publ.Google Scholar
  8. Lowry, O.H., Rosebrough, N.J., Farr, A.F., and Randall, R.J. (1951)J. Biol. Chem. 193, 265–275Google Scholar
  9. Maldonado, M.C., Navarro, A., and Callieri, D.A.S. (1986)Biotechnol. Letters 8, 501–504Google Scholar
  10. Mill, P.J., and Tuttobello, R. (1961)Biochem. J. 79, 57–64Google Scholar
  11. Moore, W.E.C., Hash, D.E., Holdeman, L.V., and Cato, P. (1980)Appl. Environm. Microbiol. 39, 900–907Google Scholar
  12. Nelson, N. (1954)J. Biol. Chem. 153, 375–380Google Scholar
  13. Somogy, M. (1952)J. Biol. Chem. 195, 19–23Google Scholar
  14. Whitaker, J.R. (1984)Enzyme Microb. Technol. 6, 341–349Google Scholar

Copyright information

© Kluwer Academic Publishers 1987

Authors and Affiliations

  • P. L. Manachini
    • 1
  • M. G. Fortina
    • 1
  • C. Parini
    • 1
  1. 1.Dipartimento di Scienze e Tecnologie Alimentari e Microbiologiche Sezione di Microbiologia IndustrialeUniversità degli Studi di MilanoMilanoItalia

Personalised recommendations