Edible insects have great potential for producing protein-rich ingredients. This study aimed to investigate the effects of protein aggregation induced by NaCl (0-1 M) and temperature (65-95 °C) on gelation of Antheraea pernyi (A. pernyi) pupa raw powder. No thermal aggregates were observed at low temperature (65 °C), on the basis of there being no significant enhancement in turbidity and particle size (P > 0.05), regardless of NaCl concentrations. At elevated temperatures (75-95 °C), protein solutions exhibited significantly higher turbidity and particle size (P < 0.05), accompanied by an initial rise in surface hydrophobicity followed by a decline, alongside declining sulfhydryl. This marks the beginning of massive thermal aggregation driven by molecular forces. In addition, covalent (disulfide bonds) and non-covalent (hydrogen bonding, electrostatic interactions, and hydrophobicity) forces were influenced by NaCl, leading to variability in the protein aggregation and gelation. Correlation analysis indicates that the higher protein aggregation induced by ions was beneficial to the construction of more compact three-dimensional structures, as well as to the rheology, texture, and water-holding capacity of A. pernyi pupa gels. However, excessive salt ions destroyed the gel structure. Our findings will aid the use of A. pernyi pupae as textural ingredients in formula foods.
Keywords: Gel; Insect proteins; Thermal aggregation.
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