Structuring high-protein foods (2012)

Increased protein consumption gives rise to various health benefits. High-protein intake can lead to muscle development, body weight control and suppression of sarcopenia progression. However, increasing the protein content in food products leads to textural changes over time. These changes result in product hardening over time and several negative sensorial attributes such as rubbery and dry mouth feel. This thesis describes the role of structuring to control the rheological and mechanical properties of high-protein model foods. By altering the internal structure of the model systems, textural properties of the model systems at initial stage (fresh products) can be improved. Content of this thesis can be distinguished into four parts. The first part reviews existing studies related to high-protein foods. The effects of ingredients and processing were evaluated with respect to food products having a high protein content. Some studies indicated typical problems occurring in products or model systems with an increased protein content such as product hardening over time. Ingredients that might be added to ameliorate product properties were plasticizers, peptides made from whey proteins, disulphide reducing agents, and components that block the free thiol groups in proteins. This part provides guidelines for structuring high-protein foods aimed at avoiding or reducing the unfavourable changes in properties over time. Concentrated proteins in their native (unmodified) form can be replaced by protein domains or structural elements with altered properties. These domains or elements mitigate the changes in product structure, resulting in a product that is softer than the one made from native proteins only. The second part focuses on the structural elements made from whey protein isolate (WPI), namely WPI aggregates and WPI microparticles. WPI aggregates were formed by different heating conditions at neutral pH. Generally, a higher concentration and a higher temperature resulted in bigger and less dense aggregates. A higher temperature also resulted in a higher reactivity (a larger number of available thiol groups). Heating an aggregate suspension led to a weaker gel than a gel made from native protein at similar. This result was hypothesized to originate from the lower number of contact points formed with larger aggregates. It was concluded that the most pronounced weakening effect could be obtained with aggregates that are large, dense, and non-reactive. That is why WPI microparticles were created. The particles were formed by gelling a concentrated WPI solution, and subsequent drying the gel and milling it into small particles. Partial replacement of native WPI with WPI microparticles resulted in a weaker gel than a gel made from native WPI only at the same total protein concentration. This result was attributed to the inability of the microparticles to form a gel. However, the weakening effect of these particles in the model system was limited due to water redistribution and the good bonding between the particles and the protein continuous phase. The third part describes how the properties of high-protein gels containing WPI microparticles change over time. A high-protein gel made from native WPI was used as a reference. The firmness and fracture stress of the gel made from WPI only increased during the first few days and then stabilized. The gel consisting of WPI microparticles in WPI or in a mixture of locust bean gum (LBG)–xanthan gum (XG) tended to harden for a longer period. Most likely, water redistribution is responsible for this observation.