Separation and Purification of Tobacco Peroxidase I from Nicotiana Tobaccum

摘要

A new isoenzyme of tobacco peroxidase(TOP) I was purified from tobacco (K326) by using acetone powder, ammonium sulfate precipitation and column chromatography on DEAF-52 cellulose, Sephadex G-75 and DEAE-Sephadex A-50. It is an iron-protein containing haemachrome, whose molecular weight is 21888.5 and the isoelectric point is 3.5. The optimum pH value and temperature of this enzyme is 6.0 and 45℃ respectively. The enzyme is stable in the pH range from 3.0 to 10.0 and has a favorable thermostability.