Partial purification and characterisation of polyphenol oxidase from celery root (Apium graveolens L.) and the investigation of the effects on the enzyme activity of some inhibitors
| dc.contributor.author | Aydemir T. | |
| dc.contributor.author | Akkanli G. | |
| dc.date.accessioned | 2025-04-10T11:17:12Z | |
| dc.date.available | 2025-04-10T11:17:12Z | |
| dc.date.issued | 2006 | |
| dc.description.abstract | Polyphenol oxidase (PPO) of celery root was extracted and partially purified by (NH4)2SO4 fractionation and dialysis. Optimum pH and temperature were found at pH 7.0 and 30°C, and Km and Vmax values were 29 mM and 5560 U mL-1 min-1 with catechol, respectively. The activation energy of the enzyme with catechol was 17.9 kJ mol-1 at pH 7.0. In electrophoretic seperation, six isoenzymes were detected with DL-dopa substrate. PPO showed activity to catechol, 4-methylcatechol, pyrogallol, gallic acid, DL-dopa. L-Tyrosine was also tested but was not oxidised by celery root PPO. β-Mercaptoethanol was found to be the most effective inhibitor. (NH 4)2SO4, NaCl, KCl and sucrose appeared to be protective agents of celery root PPO against thermal denaturation. Metal ions (Cu2+, Zn2+, Mn2+) were poor inhibitors of the celery root PPO at 1 mm. PPO activity was also inhibited by CaCl2, NaCl, BaCl2, FeSO4 and NiCl2. © 2006 Institute of Food Science and Technology Trust Fund. | |
| dc.identifier.DOI-ID | 10.1111/j.1365-2621.2006.01191.x | |
| dc.identifier.uri | http://hdl.handle.net/20.500.14701/52433 | |
| dc.publisher | Blackwell Publishing Ltd | |
| dc.title | Partial purification and characterisation of polyphenol oxidase from celery root (Apium graveolens L.) and the investigation of the effects on the enzyme activity of some inhibitors | |
| dc.type | Article |