Aydemir T.2024-07-222024-07-22201015322386http://akademikarsiv.cbu.edu.tr:4000/handle/123456789/18420Polyphenol oxidase from Rosmarinus officinalis L. (PPO, EC 1:14:18.1) was extracted and partially purified by using (NH4)2SO 4 precipitation and dialysis. Stable and highly active PPO extracts were obtained using 0.5% (w/v) PEG and 0.5% (w/v) Triton X-100 in 0.1 M phosphate buffer 7.0. KM values were found to be as 14.3 mM for catechol. Four isoenzymes of Rosemary PPO were detected by PAGE with DL-dopa substrate. The enzyme was strongly inhibited by dithiotreitol, sodium metasulfite, sodium thiosulfate, ascorbic acid, and L-cysteine. Metal ions Ca++, Mg++, and Mn++ were poor inhibitors of rosemary PPO at 10 Mm. Copyright © Taylor & Francis Group, LLC.EnglishRosmarinus officinalisCalciumDialysisKetonesManganeseManganese compoundsMetal ionsMetal refiningOrganic acidsPhenolsPolyethylene glycolsSmeltingAscorbic acidsHeat inactivationKinetic propertiesL-cysteinePH stabilityPhosphate buffersPolyphenol oxidasePoor inhibitorsRosmarinus officinalisSodium thiosulfateTriton X-100pH effectsSelected kinetic properties of polyphenol oxidase extracted from rosmarinus officinalis lArticle10.1080/10942910802641993