International Journal of Food Science and Technology, cilt.41, sa.9, ss.1090-1098, 2006 (SCI-Expanded)
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.