Hemp protein: obtaining and functional and technological properties

Abstract

The aim of this work was to determine the structural and functional characteristics of the two main hemp seed proteins, water-soluble albumin and salt-soluble globulin and alkali-soluble glutelin. The extract of 0.1 M CaCl2 protein meal of hemp seeds was subjected to sequential extraction to obtain three fractions: albumin in the aqueous phase and globulin (edestin) and glutelin in the salt phase at pH-9.0. Data on the amino acid composition showed the presence of an increased content of aromatic and hydrophobic residues in the globulin fraction. Gel electrophoresis showed that the albumin fraction had fewer disulfide bonds and therefore a more open (flexible) structure. The analysis of the content of essential amino acids in protein isolate and UV concentrate and its individual fractions was carried out for a general understanding of the ways of their application. The balance of amino acid content in the UV concentrate is close to the “ideal protein” and in the future it is advisable to use it to isolate bioactive peptides. Thus, the results obtained indicate that the processes of mechanical and chemical action on hemp flour provide raw materials with a high protein content, containing all essential amino acids and characterized by a predominant content of the sum of water and salt-soluble fractions. In connection with the identified changes in the properties of the protein obtained by different methods for release from antinutrients in the future, it is planned to pay attention to this issue separately.