%0 Journal Article %A Tzika, Evaggelia D.%A %A Sotiroudis, Theodore G.%A %A Papadimitriou, Vassiliki%A %A Xenakis, Aristotelis %D 2009 %T Partial purification and characterization of peroxidase from olives (Olea europaea cv. Koroneiki) %J European Food Research and Technology (formerly Zeitschrift Fur Lebensmittel-untersuchung und -forschung A) %V 228 %@ 1438-2377 %R 10.1007/s00217-008-0956-1 %I Springer %P 487–495 %N 3 %U https://hdl.handle.net/10442/12261 %X The enzyme peroxidase ( POD) activity was extracted from olives (Olea europaea cv. Koroneiki) and was partially purified by ammonium sulfate fractionation and gel permeation chromatography (Sephacryl S 300). Further characterization of the POD was performed using the ammonium sulfate purified fraction. POD showed a molecular mass of 44 +/- 2 kDa and it expressed catalytic activity with 2,2’-azinobis(3-ethylbenz-thiazoline-6-sulfonic acid) (ABTS), N, N-dimethyl-p-phenylenediamine (DMPD) and some olive fruit phenols. However, the enzyme was found ineffective as regards the oxidation of oleuropein, the major polyphenol of olives, as well as with coumaric, ferulic, ascorbic and p-hydroxy benzoic acids. pH optimum of the peroxidase-catalyzed oxidation depended on the substrate used and it varied from 4.0 to 6.0. Olive peroxidase shows high thermal stability. Oleuropein, the major polyphenol of olives, drastically inhibited ABTS peroxidation by the POD preparation with an IC(50) value of 47 mu M. The presence of POD enzyme activity in virgin olive oil samples was also confirmed. %> Αποθετήριο Ήλιος / ΕΙΕ