REVIEW: Palm Tree Peroxidases

I. Yu. Sakharov

Department of Chemical Enzymology, Faculty of Chemistry, Lomonosov Moscow State University, Moscow 119992, Russia; fax: (7-095) 939-2742; E-mail: sakharov@enz.chem.msu.ru

Received September 19, 2003; Revision received October 27, 2003

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Over the years novel plant peroxidases have been isolated from palm trees leaves. Some molecular and catalytic properties of palm peroxidases have been studied. The substrate specificity of palm peroxidases is distinct from the specificity of other plant peroxidases. Palm peroxidases show extremely high stability under acidic and alkaline conditions and high thermal stability. Moreover, these enzymes are more stable with respect to hydrogen peroxide treatment than other peroxidases. Due to their extremely high stability, palm peroxidases have been used successfully in the development of new bioanalytical tests, the construction of improved biosensors, and in polymer synthesis.

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KEY WORDS: peroxidase, palm tree, purification, substrate specificity, stability, application

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