| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1191633 | Food Chemistry | 2007 | 7 Pages |
Polyphenol oxidase (PPO) from broccoli florets was extracted and purified through (NH4)2SO4 precipitation, ion-exchange and gel filtration chromatography. The molecular weight was estimated to lie between 51.3 and 57 kDa by sodium dodecyl sulphate-polyacrylamide gel electophoresis (SDS-PAGE) and gel filtration. The effects of substrate specificity, pH, and sensitivity to various inhibitors: citric acid, ascorbic acid, sodium sulphate and EDTA (sodium salt of ethylenediaminetetraacetic acid) of partially purified PPO were investigated. Polyphenol oxidase showed the best activity toward catechol (KM = 12.34 ± 0.057 mM, Vmax = 2000 ± 8736 U/ml/min) and 4-methyl catechol (KM = 21 ± 0.087 mM, Vmax = 28.20 ± 0.525 U/ml/min). The optimum pH for broccoli PPO was 5.7 with catechol and 4-methylcatechol as substrates. The most effective inhibitor was sodium sulphate.
