For a number of applications, including bread-making, pasta-making, and bio-based plastics production, gluten protein polymerization and structure are of highest importance in determining end-use properties.Our results show that environmental factors contribute to a similar extent as the genetic background to protein composition and polymerization behavior in mature wheat.Most important is nitrogen availability during various phases of wheat development and the genetically determined plant development rhythm.However, the extent of importance of nitrogen availability and plant development rhythm is influenced by the temperature during the plant development time.Furthermore, a genetic component is important for polymerization of proteins during mixing.In production of bio-based plastics from wheat gluten, rearrangements of the structures and polymers of the gluten proteins are increased even further than during bread-making.Protein polymer structure was changed from a high content of unordered amide groups, and/or α-helix conformations, towards a situation where β-sheet structures of both intermolecular and extended type were common.Higher amounts of extended β-sheet structures led to outstanding characteristics of tensile strength, low protein extraction values, very low diffusion of allergy-causing proteins from the material, and low oxygen permeability in the material.Further, a hexagonal closed packed structure was found in this material.Thus, understanding how proteins are aggregating and how to combine different gluten proteins into the most suitable polymers is extremely important in both production of bread with the best baking performance and in achieving tailored materials from gluten.
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