Selected kinetic properties of polyphenol oxidase extracted from rosmarinus officinalis l
| dc.contributor.author | Aydemir T. | |
| dc.date.accessioned | 2025-04-10T11:15:44Z | |
| dc.date.available | 2025-04-10T11:15:44Z | |
| dc.date.issued | 2010 | |
| dc.description.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. | |
| dc.identifier.DOI-ID | 10.1080/10942910802641993 | |
| dc.identifier.uri | http://hdl.handle.net/20.500.14701/51245 | |
| dc.title | Selected kinetic properties of polyphenol oxidase extracted from rosmarinus officinalis l | |
| dc.type | Article |