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Purification and properties of an endopolygalacturonase produced byRhizopus stolonifer

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Summary

A polygalacturonase from culture filtrates of a strain ofRhizopus stolonifer 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.

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Authors and Affiliations

  1. Dipartimento di Scienze e Tecnologie Alimentari e Microbiologiche Sezione di Microbiologia Industriale, Università degli Studi di Milano, Via Celoria no 2, 20133, Milano, Italia

    P. L. Manachini, M. G. Fortina & C. Parini

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  1. P. L. Manachini
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  2. M. G. Fortina
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  3. C. Parini
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Manachini, P.L., Fortina, M.G. & Parini, C. Purification and properties of an endopolygalacturonase produced byRhizopus stolonifer . Biotechnol Lett 9, 219–224 (1987). https://doi.org/10.1007/BF01024570

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  • DOI: https://doi.org/10.1007/BF01024570

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