One-step purification and freeze stability of papain at acidic pH values

Papain is a proteolytic enzyme of great commercial value. It cysteine protease highly expressed in Carica papaya fruit latex, but also present leaves. Purification procedures mostly deal with the latex and include combination precipitation and/or chromatographic techniques. Due to its solubility, structure activity characteristics, pH salt content play significant roles handling papain extracts. Here we report simple, rapid easily scalable procedure for purification from leaves, which contain different contaminants as compared latex. Sodium chloride at 5 followed by ammonium sulphate resulted removal other leaf proteins protein fragments solution about 3-fold purification. The benefits suppression autoproteolysis preservation native structure, confirmed FTIR analysis, high recovery over 80%.