Impact of High Hydrostatic Pressure on the Physicochemical Characteristics, Functional Properties, Structure, and Bioactivities of <scp><i>Tenebrio molitor</i></scp> Protein

This study aimed to explore the influence of high hydrostatic pressure (HHP) treatment on the structure, functional characteristics, and bioactivities of <i>Tenebrio molitor</i> protein. The results showed that HHP induced dissociation of <i>T. molitor</i> 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 <i>T. molitor</i> 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 <i>T. molitor</i> protein, as demonstrated by circular dichroism and fluorescence spectra. Furthermore, HHP treatment significantly affected the antibacterial and antioxidant activities of <i>T. molitor</i> protein. This study provides a theoretical framework for using HHP to modify <i>T. molitor</i> protein.