ISHS Acta Horticulturae 681: IV International Congress on Artichoke
CHARACTERIZATION AND PARTIAL PURIFICATION OF PEROXIDASE FROM ARTICHOKE LEAVES |
| Authors: | A. Cardinali, D. Di Venere, L. Sergio, V. Linsalata |
| Keywords: | Cynara cardunculus, soluble, ionically bound and covalently bound peroxidases, affinity chromatography, AE-HPLC |
| Abstract:
Artichoke, Cynara cardunculus L. subsp. scolymus (L.) Hayek, is widely used in processed food industry. Leaves and external bud bracts discarded as refuse represent about 70% of the total biomass and could be utilized to extract important compounds as phenols and enzymes (i.e. polyphenoloxidase and peroxidase) very abundant in this vegetable. Peroxidases (PODs) are part of a large group of enzymes associated with cell wall biosynthesis, response to injury, disease, resistance and wound repair. In this study the separation and distribution of soluble peroxidase (SP), ionically bound (IBP) and covalently bound (CBP) peroxidases from artichoke leaves was performed. The POD forms were analyzed by SDS-PAGE and stained for peroxidase activity using o-dianisidine as substrate. The SP and IBP electrophoretic patterns were very similar. They showed three different molecular weight (MW) zones: 100 KD, 60 KD and 35 KD. The CBP pattern was different; it showed a group of high MW bands. The SP was partially purified by ammonium sulfate precipitation, gel filtration, affinity chromatography and AE-HPLC. The increase of specific activity was 43 fold compared to the crude extract as estimated by the guaiacol assay. The SDS-PAGE stained for POD activity showed a double band with an apparent MW of about 60 KD. | |
Download Adobe Acrobat Reader (free software to read PDF files) | |
