LAUSR

This study focused on the extraction, purification and physicochemical characterization of γ-conglutin, a protein present in lupin seeds with properties of reducing blood glucose levels. Total protein was extracted with alkaline-saline solvent, followed by isoelectric precipitation. Chromatographic purification of the precipitated fraction was performed using a cation exchange supermacroporous cryogel column. Electrophoresis of the eluted fraction from chromatography presented a single band of ∼48 kilodaltons under non-reducing conditions (two bands of ∼30 and 17 kilodaltons, under reducing conditions) confirming the success of the purification protocol. LC-MS/MS analysis confirmed the identity of the protein as γ-conglutin. The purified γ-conglutin had an isoelectric point of 7.51, β-sheets prevailing as a secondary structure and denaturation temperature close to 68 °C. The outcome of this work showed that γ-conglutin was obtained with high degree of purity. The proposed purification protocol is simple and can be easily scaled up. This article is protected by copyright. All rights reserved.