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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
Article

Summary

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.

Keywords

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.

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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

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