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.
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