4.7 Article

Purification and properties of a neutral peroxidase isozyme from turnip (Brassica napus L. var. purple top white globe) roots

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JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 49, 期 9, 页码 4450-4456

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AMER CHEMICAL SOC
DOI: 10.1021/jf010043e

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neutral peroxidase; turnip roots; protein purification

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A neutral peroxidase isozyme (pI 7.2) from turnip roots (TNP) was purified to homogeneity and partially characterized. TNP is a monomeric glycoprotein with 9.1% carbohydrate content and a molecular 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 K-m values were 0.7 and 3.7 mM, respectively. The ABTS K-m was similar to7 times higher than that reported for basic commercial horseradish peroxidase (HRP-C). TNP retained similar to 70% activity after 11 min of heating at 65 degreesC, whereas the activation energy for inactivation (132 kJ/mol) was higher than or comparable to that of other peroxidases. The low ABTS K-m and high specific activity (1930 units/mg) gave a high catalytic efficiency (500 M-1 s(-1)). These properties make TNP an enzyme with a high potential as an alternative to HRP in various applications.

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