Assessing the emulsifying properties of Tenebrio molitor larvae protein preparations: Impact of storage, thermal, and freeze-thaw treatments on o/w emulsion stability.

Insect proteins have gained attention as novel ingredients, which may contribute to the development of high-value-added products. This study evaluates the emulsifying and emulsion-stabilizing properties of Tenebrio molitor larvae protein preparations obtained through different procedures, leading to the following rich-in-protein samples: ASP (∼67 %), AIP (∼75 %), and SSP (∼62 %). The method applied for protein isolation influenced the molecular and structural characteristics of the preparations, thus affecting their adsorption behaviour at oil-water interfaces and ability to stabilize emulsions. O/w emulsions were prepared, and their physicochemical stability was assessed with respect to droplet size, oil droplet flocculation/coalescence, microstructure, and creaming upon storage as well as after thermal and freeze-thaw treatments. The use of ASP and AIP protein preparation as emulsifiers led to higher stability during storage. All emulsions were stable upon heating and able to withstand two freeze-thaw cycles without phase separation, although there was an increase in droplet size. Interestingly, the AIP emulsion remained stable after the 3rd freeze-thaw cycle, indicating remarkable stability under freezing compared to the other two emulsions. These findings are of great importance for the formulation of food-grade emulsions using insect protein preparations and their future exploitation in developing food items subjected to different treatments.

Characterization of Tenebrio molitor Larvae Protein Preparations Obtained by Different Extraction Approaches.

Edible insects have recently attracted research attention due to their nutritional value and low environmental footprint. Tenebrio molitor larva was the first insect species to be classified by European Food Safety Authority (EFSA) as safe for human consumption. However, it is thought that the incorporation of edible insect as an ingredient in a food product would be more appealing to consumers than being visible. The aim of the present study was to determine the physicochemical properties of the larvae meal and protein concentrates. Different methods to extract and recover proteins from defatted (DF) Tenebrio molitor larvae were applied; i.e., alkaline extraction (DF-ASP); isoelectric precipitation after alkaline extraction (DF-AIP); and NaCl treatment (DF-SSP), and the obtained protein fractions were characterized. The DF-ASP exhibited the highest protein extraction/recovery efficiency (>60%), while it was the most effective in decreasing the interfacial tension at the oil/water (o/w) interface. The DF-AIP had the highest protein content (75.1%) and absolute values of ζ-potential and the best ability to retain water (10.54 g/g) and stabilize emulsions at pH 3.0. The DF-SSP protein preparation had the highest oil binding capacity (8.62%) and solubility (~88%) at acidic pHs and the highest emulsifying activity (~86 m2/g). Electrophoresis of the protein preparations revealed proteins with different molecular weights, while the protein secondary structure was dominated by ß-structures and α-helix. Protein concentrates with different properties were able to be recovered from Tenebrio molitor larvae, that could affect their interactions with other food ingredients and their behavior during processing or storage. These findings would be valuable guidance for the technological exploitation of larvae protein preparations in the development of food formulations.