Globular proteins influence protein network formation in and quality of wheat-based noodles

To address the demand for healthy protein-rich food, nutritious protein sources (e.g. egg, soy or milk) are sometimes included in wheat noodle recipes. Interactions and reactions between different types of proteins can impact complex food systems and are referred to as co-protein effects. They can be synergistic or antagonistic. The relation between protein characteristics, protein network formation and wheat noodle properties was studied. Globular model protein such as bovine serum albumin (BSA), soy glycinin, hen egg ovalbumin, S-ovalbumin and lysozyme were included in the recipe of wheat-based noodles. The characteristics of these non-wheat proteins impacted the type, rate and extent of protein network formation during noodle dough preparation and boiling, and thereby the properties of fresh (i.e. raw) and boiled noodles. None of the added proteins enhanced the properties of fresh noodles. BSA and soy glycinin enhanced Kieffer-rig extensibility parameters of cooked noodles. Addition of ovalbumin or S-ovalbumin led to excessive protein polymerization in cooked noodles and lowered their extensibility and cooking quality. Inclusion of lysozyme lowered the rate and extent of polymerization during boiling. Experiments in which salt, olive oil or urea were added in the recipe showed that non-covalent interactions dominate the properties of fresh noodles while covalent cross-links and hydrogen bonds mainly impact the properties of boiled noodles. In addition, synergistic or antagonistic co-protein effects of binary proteins mixtures in model systems were linked to the rate/extent of polymerization, optimal cooking time, cooking quality and Kieffer-rig extensibility of wheat-based noodles. Proteins from different sources cannot only enhance the nutritional value but also the quality of wheat-based noodles.status: publishe