Partial purification and thermal stability of two peroxidases from Pithecellobium dulce (Roxb.) Benth. Aril

Abstract

Two peroxidase (POX) forms, named PdPI and PdPII, were partially purified from the Pithecellobium dulce aril, using ammonium sulfate precipitation and anion exchange chromatography. Zymography of the proteins obtained after precipitation in the range of 60-90% ammonium sulfate (F6090 fraction) showed two bands with peroxidase activity. In DE-52 cellulose column, the peroxidase activity was detected in unadsorbed peak (PdPI) and adsorbed peak eluted with 0.2 mol L-1 NaCl (PdPII) suggesting that PdPI (∼114 KDa) and PdPII (∼77 KDa) are basic and acidic proteins, respectively, being PdPI stable at 80 °C. This is the first report of partial purification of POX from P. dulce aril, indicating that this species may be a new source of enzymes for use in biosensors and other biotechnological applications.