Redox agents and N-ethylmaleimide affect the extractability of gluten proteins during fresh pasta processing

Abstract

The gluten protein network is of great importance for pasta cooking quality. Redox agents were used as a tool to impact the protein network formation during laboratory scale fresh pasta making (mixing and sheet rolling) and cooking. SE- and RP-HPLC data showed that disulphide bonds are formed in the pre-existing gluten protein network during cooking of fresh pasta and that, in the process, glutenin polymerisation occurs faster than gliadin–glutenin copolymerisation. The thiol blocking agent N-ethylmaleimide (245ppm, expressed on semolina, dry basis) and, to a lesser extent, the oxidising agent potassium iodate (70ppm), hindered glutenin polymerisation and gliadin–glutenin copolymerisation during cooking. However, the introduction of reactive thiol groups, by addition of the reducing agent glutathione (100ppm), resulted in faster gliadin–glutenin copolymerisation during cooking.