[en] Corn (Zea mays L.) is the most abundant cereal grain produced in the world. It also provides a significant amount of protein in human and animal diets. During drying corn grains undergo several alterations including protein denaturation. A series of studies have been conducted in order to understand mechanisms behind denaturation of corn proteins during drying and heat moisture treatments. Using a laboratory fluidized-bed dryer, a flint corn variety have been dried between 54° and 130°C and subjected to different analyses from a qualitative point of view with a sequential extraction of corn protein fractions and from a quantitative point of view with the modeling of salt-soluble proteins using Promatest assay. Albumin, globulin and zein solubilities dropped significantly when the drying temperature increased. The electrophoretic patterns of zein and glutelin-G1 were not significantly modified, although the solubility of zein was affected by the drying temperature. The analysis of the different protein group solubilities suggested that denaturation mechanisms other than the creation of new disulfide bonds occurred during the drying of corn at high temperature. The study of the effect of heat treatments on the extractability of salt-soluble proteins shows that temperature; moisture content and time of processing greatly influence their kinetic denaturation. Modeling of salt-soluble proteins reveals that the evolution of extractible salt-soluble proteins content of corn kernels during drying at high temperature is more correctly described with a second order kinetic reaction. Investigations continue in order to understand protein denaturation and influence in functional properties and end-use of corn protein-based products.
