How does the thermal-aggregation behavior of black cricket protein isolate affect its foaming and gelling properties?

Edible insects are a promising source of high-quality proteins and their use to produce protein-rich ingredients for formulated foods has been pointed out as a good alternative to increase their acceptance by consumers. In order to understand the technological potential of these novel ingredients, it is crucial to characterize their behavior during food processing. In this context, this study aimed to evaluate the effect of heat treatments (65, 75, 85, 90 and 95 degrees C for 15 min) at variable ionic strength (from 0 up to 0.5 M of NaCl) on the structure, gelling and foaming properties of black cricket (Gryllus assimilis) protein isolate (BCPI). In absence of added NaCl, heat treatments do not considerably change the secondary structure of the proteins, although leaded to an increase of their surface hydrophobicity. On the other hand, heat treatment in the presence of NaCl induced a decrease in the content of the alpha-helix structure and the surface hydrophobicity of the proteins. The foamability of heat treated (at 75 and 95 degrees C for 15 min) dispersions supplemented or not with NaCl was similar to the one of whey protein isolate (WPI) dispersion. In addition, the BCPI dispersion heat treated at 90 degrees C for 15 min had a critical gelling concentration of 6.5% w/w, also comparable to WPI, which reveals its technological potential for food applications.

Automated summary

This study evaluated the impact of heat treatments on the structure, gelling, and foaming properties of black cricket protein isolate (BCPI), showing that heat treatments can alter the hydrophobicity of proteins and that the presence of NaCl can reduce the alpha-helix structure content. Additionally, BCPI demonstrated similar foamability and critical gelling concentration to whey protein isolate (WPI), indicating its potential for food applications.