Extraction And Purification Of Peroxidase And Trypsin Inhibitor From Soybean Hulls: A Strategy To Revalue A Waste As A Source Of Different Types Of Molecules Of Biotechnological Interest

In this work, the extraction and purification of proteins present in soybean hull has been carried out, using simple methods and with the potential to be scaled. In the first stage, using statistical tools, the optimization of peroxidase extraction and various protease inhibitor factors was achieved through a leaching process using 50 mM phosphate buffer pH 6.00. The optimal conditions to achieve the best extraction of the proteins of interest were the following: contact time (360 min), mass/volume ratio (0.066) and particle size (40 mesh). The extract obtained was characterized by an electrophoresis gel, mass spectrometry and by measuring enzymatic activity, which, allowed to confirm the presence of the proteins of interest. Finally, the purification of peroxidase and protease inhibitors were optimized by adsorption onto aminated cellulose bed obtained from the same soybean hull. Under the optimal conditions, the peroxidase present in the extract was purified 8.1 times with a yield of 66.6%. While protease inhibitors were purified 2.5 times with a yield of 26.1%.