Exopolygalacturonase in tomato fruit |
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| Affiliation: | 1. The University of Texas at Austin, Department of Civil, Architectural and Environmental Engineering, 301 E. Dean Keeton St. Stop C1761, Austin TX 78712, USA;2. King Abdulaziz University, Jeddah 21589, Saudi Arabia;3. King Abdulaziz University, Department of Civil Engineering, P.O. Box 80204, Jeddah 21589, Saudi Arabia;1. Pronto Soccorso/D.E.A. - Chiari-Iseo (BS) ASST Franciacorta, viale Giuseppe Mazzini 4, 25032 Chiari (Brescia), Italy;2. Terapia Intensiva Neonatale ASST Spedali Civili (Brescia), Piazzale Spedali Civili 1, 25123 Brescia (BS), Italy;3. Cardiologia Ospedale San Vincenzo - Taormina (Me) Azienda Sanitaria Provinciale di Messina, Contrada Sirina, 98039 Taormina (Messina), Italy |
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| Abstract: | A low level of polygalacturonase has been found in unripe tomato fruit. The enzyme was extracted with 0.5 M NaCl containing 0.05 M CaCl2, concentrated by ultrafiltration and purified 150-fold by ion-exchange chromatography. The M, of the enzyme was 47 000. It was optimally active at pH 5 and required Ca2+ for activity, with an optimum concentration of 0.42 mM Ca2+. The enzyme has been characterized as an exopolygalacturonase that cleaves monomer units from the non-reducing ends of the substrate molecules. The optimum substrate size for the enzyme was that with a degree of polymerization of ca 13. The amount of exopolygalacturonase activity remained essentially constant during development and ripening of the fruit. |
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