Data di Pubblicazione:
1987
Citazione:
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.
Abstract:
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.
Tipologia IRIS:
01 - Articolo su periodico
Elenco autori:
P.L. Manachini, M.G. Fortina, C. Parini
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