Abstract
The objective of this study was to explore the impacts of various ultrasonic powers (0, 300, 500, 700, and 900 W) on the structure and functional attributes of the myofibrillar protein (MP) of Tenebrio molitor. As the ultrasonic intensity escalated, the extraction efficiency and yield of the MP rose, while the particle size and turbidity decreased correspondingly. The reduction in sulfhydryl group content and the increase in carbonyl group content both suggested that ultrasonic treatment promoted the oxidation of the MP to a certain extent, which was conducive to the formation of a denser and more stable gel network structure. This was also affirmed by SEM images. Additionally, the findings of intrinsic fluorescence and FTIR indicated that high-intensity ultrasound significantly altered the secondary structure of the protein. The unfolding of the MP exposed more amino acid residues, the α-helix decreased, and the β-helix improved, thereby resulting in a looser and more flexible conformation. Along with the structural alteration, the surface hydrophobicity and emulsification properties were also significantly enhanced. Besides that, SDS-PAGE demonstrated that the MP of T. molitor was primarily composed of myosin heavy chain (MHC), actin, myosin light chain (MLC), paramyosin, and tropomyosin. The aforementioned results confirmed that ultrasonic treatment could, to a certain extent, enhance the structure and function of mealworm MP, thereby providing a theoretical reference for the utilization of edible insect proteins in the future, deep-processing proteins produced by T. molitor, and the development of new technologies.