Modification of plant-derived food proteins via enzymatic treatment to improve organoleptic features

This research is focused on the use of transglutaminases (TGs) for the biotechnological treatment of gluten-free flours in order to obtain a baked product (e.g., bread) suitable for people affected by Celiac Disease (CD) and Non Celiac Gluten Sensitivity (NCGS). TGs are a family of enzymes that catalyse the formation of isopeptide bonds between a protein-bound glutamine residue and a protein-bound lysine residue. The reaction produces stable linkages resulting in the formation of high-molecular-weight complexes forming large protein networks. One of the main problems associated with gluten-free baked products is obtaining a good structure. Surface lysine and glutamine residues are important in the formation of cross-links and indeed in the improvement of the texture of food proteins. Thanks to its features, TGs could improve the structure of gluten-free breads. Moreover, TGs are able to covalently incorporate primary amines into protein-bound glutamine residues, thereby modifying the nutritional value of the final product via the incorporation of proteins or peptides containing essential amino acids.