Insights into the construction of binary protein systems and exploration of gel properties: Effect of bee pupa powder on the gel properties of myofibrillar protein from Litopenaeus vannamei.

This investigation elucidated the effects of bee pupa powder (BPP) incorporation on the gelation behavior of Litopenaeus vannamei myofibrillar protein (MP), utilizing advanced microstructural analyses and molecular interaction assessments. Laser confocal microscopy revealed a homogeneous dispersion of BPP within the surimi matrix, with optimal BPP: MP ratios (1:20, w/w) facilitating the unfolding of tertiary protein structures through enhanced hydrophobic interactions and disulfide bond formation, thereby reinforcing the three-dimensional gel network. Beyond this threshold, steric hindrance effects predominated, diminishing interfacial interactions and gel integrity. Notably, BPP supplementation improved the proteolytic digestibility of dual-protein gels, suggesting enhanced nutrient bioaccessibility. These findings advance strategies for insect-protein utilization while providing mechanistic insights for the development of texture-optimized, nutritionally fortified marine hybrid gels.