Some kinetic properties of polyphenol oxidase obtained from dill (Anethum graveolens).
Polyphenol oxidase (PPO) was partially purified from dill by (NH4)(2)SO4 precipitation followed by dialysis and gel filtration chromatography. Polyphenol oxidase activity was measured spectrophotometrically at 420 nm using catechol, dopamine and chlorogenic acid as substrates. Optimum pH, temperature, and ionic strength were determined with three substrates. The best substrate of dill PPO was found to be chlorogenic acid. Some kinetic properties of the enzyme such as V(max,) K(M) and V(max)/K(M) were determined for all three substrates. The effects of various inhibitors on the reaction catalysed by the enzyme were tested and I(50) values calculated. The most effective inhibitor was L-cysteine. Activation energies, E(a), were determined from the Arrhenius equation. In addition, activation enthalpy, DeltaH(a), and Q(10) values of the enzyme were also calculated.
Department of Chemistry, Faculty of Arts and Sciences, Ataturk University, Erzurum, Turkey. hsakir@atauni.edu.tr
Halis
H
Sakiroğlu
Ahmet Emin
AE
Oztürk
Anil Ece
AE
Pepe
Mustafa
M
Erat
D028524:Anethum graveolens / Q000201:enzymology*; D004156:Catechol Oxidase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D002726:Chlorogenic Acid; D003545:Cysteine; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009994:Osmolar Concentration; D010940:Plant Proteins; D013379:Substrate Specificity; D013696:Temperature; D013816:Thermodynamics
D010940:Plant Proteins; D002726:Chlorogenic Acid; D004156:Catechol Oxidase; D003545:Cysteine