RESUMEN
The use of whole and visible insects is poorly accepted in Western countries, and this remains a significant challenge for product development. However, using insect-based protein-rich ingredients, like protein concentrate, can improve levels of consumer approval. The residual lipid content in insect protein concentrates can influence their techno-functional properties. Our study therefore aimed to evaluate the impact of the residual lipid content on the protein structure and foaming properties of a mealworm protein concentrate. Our results showed that the protein content increased from 78.01 to 84.82 % after using chloroform-methanol for lipid removal. The particle size distribution shifted from a bimodal to a unimodal pattern, and the surface hydrophobicity decreased from 267.02 to 48.91 after completely removing lipids by chloroform-methanol, with no noticeable impact on the protein profile. The foaming capacity improved, resulting in the formation of a firm and fluffy foam with high stability over time. These results highlight the importance of controlling the residual lipid content in mealworm protein concentrates to enhance their techno-functional properties. The next steps will entail comprehensively characterizing the lipid profile and exploring the various mechanisms contributing to the techno-functional properties.
RESUMEN
Edible insects represent a great alternative protein source but food neophobia remains the main barrier to consumption. However, the incorporation of insects as protein-rich ingredients, such as protein concentrates, could increase acceptance. In this study, two methods, isoelectric precipitation and ultrafiltration-diafiltration, were applied to produce mealworm protein concentrates, which were compared in terms of composition, protein structure and techno-functional properties. The results showed that the protein content of the isoelectric precipitation concentrate was higher than ultrafiltration-diafiltration (80 versus 72%) but ash (1.91 versus 3.82%) and soluble sugar (1.43 versus 8.22%) contents were lower. Moreover, the protein structure was affected by the processing method, where the ultrafiltration-diafiltration concentrate exhibited a higher surface hydrophobicity (493.5 versus 106.78 a.u) and a lower denaturation temperature (161.32 versus 181.44 °C). Finally, the ultrafiltration-diafiltration concentrate exhibited higher solubility (87 versus 41%) and emulsifying properties at pH 7 compared to the concentrate obtained by isoelectric precipitation.
