Abstract

Purification of low abundance enzymes for biochemical characterization is frequently labor and cost-intensive. The existence of co-expressing multigene families increases the complexity of the procedure even further as it occurs with plant peroxidases where only the most abundant species have been studied. In this paper we present an optimized purification method for Zo peroxidase, a low abundance isoenzyme with unusual tolerance to hydrogen peroxide. This protocol is straightforward, allowing the purification of the enzyme at milligram levels in 10 days. Furthermore, the protocol may be easily adapted for the direct purification of other non abundant peroxidase isoenzymes from plant tissues.

Key words: Peroxidase, hydrogen peroxide, desactivation, Japanese radish.