A neutral peroxidase isozyme (p
I 7.2) from turnip roots (TNP) was purified to homogeneity andpartially characterized. TNP is a monomeric glycoprotein with 9.1% carbohydrate content and amolecular weight of 36 kDa. Optimum pH values for activity using 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid (ABTS) and guaiacol as H donors were 4.5 and 5.5, whereas the
Km valueswere 0.7 and 3.7 mM, respectively. The ABTS
Km was ~7 times higher than that reported for basiccommercial horseradish peroxidase (HRP-C). TNP retained ~70% activity after 11 min of heatingat 65
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C, whereas the activation energy for inactivation (132 kJ/mol) was higher than or comparableto that of other peroxidases. The low ABTS
Km and high specific activity (
1930 units/mg) gave ahigh catalytic efficiency (500 M
-1 s
-1). These properties make TNP an enzyme with a high potentialas an alternative to HRP in various applications.Keywords: Neutral peroxidase; turnip roots; protein purification