Purification and characterization of polyphenol oxidase from Ferula sp.
作者： M ERAT , H SAKIROGLU , O KUFREVIOGLU
DOI: 10.1016/J.FOODCHEM.2005.01.044
关键词:
摘要: Abstract Polyphenol oxidase (PPO) of several Ferula sp. was extracted and purified through (NH 4 ) 2 SO precipitation, dialysis, gel filtration chromatography. Leaf stem extracts were used for the determination enzyme properties. Optimum conditions, pH, temperature, ionic strength determined. The best substrates PPO catechol leaf (−) epicatechin samples. pH temperature K M V max values 2.34 × 10 −3 M 8541 EU/ml catechol, 2.89 × 10 5308 EU/ml epicatechin. most effective inhibitor sodium diethyl dithiocarbamate samples metabisulphite Both inhibitors indicated competitive reactions. showed irreversible denaturation after 40 min at 60 °C.
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