Thermal stability and rheological properties of heat-induced gels prepared using edible insect proteins in a model system

We investigated the thermal stability and rheological properties of heat-induced gels prepared using edible insect proteins originating from various edible insect species: Tenebrio molitor L., Protaetia brevitarsis larvae, and Allomyrina dichotoma larvae. The protein solubility and pH of the heat-induced gel prepared from A. dichotoma exhibited the highest value (P < 0.05) among all samples. The redness and yellowness (P < 0.05); water holding capacity (P < 0.05); and springiness, cohesiveness, gumminess, and chewiness (P < 0.05) of the heat-induced gel from P. brevitarsis showed the highest values. The apparent viscosity of the gel from P. brevitarsis was higher than that of the other samples (P < 0.05). The storage modulus (G') and loss modulus (G '') of the gel from T. molitor were lower than those of the gel from P. brevitarsis and A. dichotoma. Compared to the edible insect proteins obtained from T. molitor, those from P. brevitarsis and A. dichotoma were more heat stable, with a more complex structure, and showed various peak temperatures. P. brevitarsis and T. molitor gels displayed the highest and lowest emulsion capacity, respectively (P < 0.05). Thus, the gels from P. brevitarsis and A. dichotoma proteins exhibited excellent processing functionalities as heat-induced gels.