Changes in durum wheat kernel and pasta proteins induced by toasting and drying processes

Durum wheat kernels were subjected to a toasting process and the proteins characterised by size exclusion-high performance liquid chromatography (SE-HPLC) and sodium dodecyl sulphate–polyacrylamide gel electrophoresis. With this physical process, albumins and globulins, as well as glutenins and gliadins, polymerised as seen by a shift of the SE-HPLC profile to lower elution times. The polymerisation seemed to happen mainly through disulphide bonds, even though the participation of ω-gliadins to the aggregation suggested the involvement of other kinds of interactions. It led to the revelation of a new peak originated by thermal aggregation of small polymeric proteins. The changes in the chromatographic profile were accompanied by increasing amounts of total unextractable polymeric proteins. The replacement of semolina with toasted durum wheat flour (5%, 10%, 15%, 20% and 30%) for the production of pasta in the shape of spaghetti significantly (p < 0.001) affected the molecular size distribution of the polymeric proteins, even though the replacement of semolina with 5% and 10% of toasted durum wheat flour (TDWF) did not significantly (p > 0.05) change the unextractable polymeric proteins (UPP) when compared with spaghetti made with 100% durum semolina. On the other hand, the replacements of semolina with 15–30% TDWF showed significant (p < 0.001) increase in UPP when compared with 100% durum semolina spaghetti.