A comparative study of the structural and functional properties of isolated hemp seed (Cannabis sativa L.) albumin and globulin fractions

Abstract The aim of this work was to determine the structural and functional characteristics of two major hemp seed proteins, the water-soluble albumin (ALB) and the salt-soluble globulin (GLB). The 0.5 M NaCl extract of hemp seed protein flour was dialyzed against water to obtain the two fractions: ALB in the water phase and GLB in the insoluble precipitate. The protein fractions were subjected to structural (gel electrophoresis, intrinsic fluorescence and circular dichroism) and functional (protein solubility, foaming, and emulsion) tests. Amino acid composition data showed the presence of higher contents of aromatic and hydrophobic residues in GLB. Gel electrophoresis indicated that the ALB has less disulfide bonds and hence a more open (flexible) structure; this was confirmed by the intrinsic fluorescence and circular dichroism data showing greater exposure of tyrosine residues when compared to GLB. ALB had significantly ( p