Purification of Peroxidase Enzyme from Water Mimosa by Chromatography Technique.

<b>Background and Objective:</b> Peroxidase (POD) is the most widely used enzyme in the manufacture of diagnostic kits, biosensors, immunohistochemistry and different industrial sectors. In this study, the POD was extracted from some local vegetables in Thailand; water mimosa. The POD was biochemically purified and characterized from water mimosa.

Bifunctional activity of fused Plasmodium falciparum orotate phosphoribosyltransferase and orotidine 5'-monophosphate decarboxylase.

Fusion of the last two enzymes in the pyrimidine biosynthetic pathway in the inversed order by having a COOH-terminal orotate phosphoribosyltransferase (OPRT) and an NH-terminal orotidine 5'-monophosphate decarboxylase (OMPDC), as OMPDC-OPRT, are described in many organisms. Here, we produced gene fusions of Plasmodium falciparum OMPDC-OPRT and expressed the bifunctional protein in Escherichia coli. The enzyme was purified to homogeneity using affinity and anion-exchange chromatography, exhibited enzymatic activities and functioned as a dimer.