Purification of model solutions from copper(2+) ions with aqueous extracts from hydrolysates of protein-containing keratin

Abstract

A hydrolysate based on keratin-containing raw materials (sheep wool) was obtained by alkaline hydrolysis. The optimal conditions of the hydrolysis process have been established. IR spectroscopic studies have shown that the assumed structure of the samples corresponds to the content of amino acids with a peptide bond in them. The experiments have determined that the greatest degree of removal of copper ions from model solutions, with a concentration of these ions of 1 mol/l, is observed when an aqueous extract from sheep wool keratin hydrolysate is added. It was found that the greatest decrease in the concentration of Cu2+ ions was observed when the extract was added to the 4 cm3 model solution and the removal of ions was 82%. The formation of amino acids with copper ions by internal complex compounds was revealed, in which the Cu(II) atom is associated with oxygen and nitrogen atoms of amino groups. In this case, chelate structures consisting of five-membered cycles arise.