Purification and characterization of polyphenol oxidase from Ferula sp.

被引：47

作者：

Erat, M ^{[1
]}

Sakiroglu, H ^{[1
]}

Kufrevioglu, OI ^{[1
]}

机构：

[1] Ataturk Univ, Fac Arts & Sci, Dept Chem, TR-25240 Erzurum, Turkey

来源：

FOOD CHEMISTRY | 2006年 / 95卷 / 03期

关键词：

polyphenol oxidase; Ferula sp; kinetics;

D O I：

10.1016/j.foodchem.2005.01.044

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

Polyphenol oxidase (PPO) of several Ferula sp. was extracted and purified through (NH4)(2)SO4 precipitation, dialysis, and gel filtration chromatography. Leaf and stem extracts were used for the determination of enzyme properties. Optimum conditions, for pH, temperature, and ionic strength were determined. The best substrates of PPO were catechol for leaf and (-) epicatechin for stem samples. Optimum pH and temperature were determined. K-M and V-max, values were 2.34 x 10(-3) M and 8541 EU/ml for catechol, and 2.89 x 10(-3) M and 5308 EU/ml for (-) epicatechin. The most effective inhibitor was sodium diethyl dithiocarbamate for leaf samples and sodium metabisulphite for stem samples. Both inhibitors indicated competitive reactions. PPO showed irreversible denaturation after 40 min at 60 degrees C. (c) 2005 Elsevier Ltd. All rights reserved.

引用

页码：503 / 508

页数：6

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