Tenebrio molitor powder enhances gelation properties of Penaeus vannamei myofibrillar protein: Mechanistic insights into structural optimization and digestibility.

The study aimed to investigate how Tenebrio molitor powder (TMP) influences the gelation properties of Penaeus vannamei myofibrillar protein, specifically seeking to identify optimal TMP-to-protein ratios. TMP: myofibrillar protein ratios (1:40, 1:20, 1:10) were evaluated through texture analysis, rheological testing, water-holding capacity (WHC), and microstructure observation. Texture analysis revealed a 27.7 % increase in rupture strength (272.3 g·mm) at the 1:20 ratio compared to myofibrillar protein. Rheological assessments indicated peak viscosity and viscoelastic moduli for the 1:20 group, demonstrating enhanced gel elasticity. The WHC reached a maximum value of 78.5 % in the 1:20 group due to improved water binding interactions. Confocal microscopy confirmed a uniform three-dimensional network at the 1:20 ratio, while excessive TMP (1:10) disrupted hydrophobic interactions and compromised gel integrity. TMP also improved the in vitro gel digestibility by reducing undigested particle size. These findings demonstrate TMP's potential for tailoring surimi gel quality through controlled protein interactions.