This study aimed to explore the influence of high hydrostatic pressure (HHP) treatment on the structure, functional characteristics, and bioactivities of Tenebrio molitor protein. The results showed that HHP induced dissociation of T. molitor protein, exposing hydrophobic groups and reducing particle size, which in turn reduced turbidity. Additionally, 600 MPa treatment significantly reduced the foaming stability and emulsifying activity of T. molitor protein. Treatments at 200 MPa and 400 MPa significantly reduced emulsion stability, whereas 400 MPa treatment significantly increased oil retention. HHP treatment also altered the secondary and tertiary structures of T. molitor protein, as demonstrated by circular dichroism and fluorescence spectra. Furthermore, HHP treatment significantly affected the antibacterial and antioxidant activities of T. molitor protein. This study provides a theoretical framework for using HHP to modify T. molitor protein.
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Zhang et al. (2025) studied this question.
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