A polygalacturonase from culture filtrates of a strain of Rhizopus 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 mol/ g/min. In addition, this enzymatic preparation degraded pectic substances in orange peel.
Purification and properties of an endopolygalacturonase produced by Rhizopus stolonifer / P.L. Manachini, M.G. Fortina, C. Parini. - In: BIOTECHNOLOGY LETTERS. - ISSN 0141-5492. - 9:3(1987), pp. 219-224.
|Titolo:||Purification and properties of an endopolygalacturonase produced by Rhizopus stolonifer|
MANACHINI, PIER LUIGI (Primo)
FORTINA, MARIA GRAZIA (Secondo)
PARINI, CARLO (Ultimo)
|Settore Scientifico Disciplinare:||Settore AGR/16 - Microbiologia Agraria|
|Data di pubblicazione:||1987|
|Digital Object Identifier (DOI):||http://dx.doi.org/10.1007/BF01024570|
|Appare nelle tipologie:||01 - Articolo su periodico|