Selected kinetic properties of polyphenol oxidase extracted from rosmarinus officinalis l
Abstract
Polyphenol 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.
Description
Keywords
Rosmarinus officinalis , Calcium , Dialysis , Ketones , Manganese , Manganese compounds , Metal ions , Metal refining , Organic acids , Phenols , Polyethylene glycols , Smelting , Ascorbic acids , Heat inactivation , Kinetic properties , L-cysteine , PH stability , Phosphate buffers , Polyphenol oxidase , Poor inhibitors , Rosmarinus officinalis , Sodium thiosulfate , Triton X-100 , pH effects