In this study, we first developed an efficient and eco-friendly expression system of the recombinant hydrophobin HGFII-his by introducing the POT1-mediated δ sequences site-specific integration strategy in Saccharomyces cerevisiae. Furthermore, according to the physical measurements, Sc-HGFII-his (expressed by S. cerevisiae) and Pp-HGFII-his (expressed by Pichia pastoris strain GS115) revealed identical selfassembly and surface modification properties. Subsequently, we confirmed that the Sc-HGFII-his self-assembled to globular morphology instead the classic rodlets of class I hydrophobins. Additionally, the HGFII-his-based curcumin nanoformulations revealed the nanoparticle profile and were capable of sustained release of curcumin for at least 72 h. As expected, they exhibited satisfied cell uptake profiles and dramatically cytotoxic activity against HeLa cells in antitumor assays. These findings indicate that HGFII-his was suitable for pharmaceutical emulsion formulations. Herein, we pushed the boundaries of an efficient method for the HGFII-his production, realized sustained curcumin release, and boosted the bioavailability and efficacy with HGFII-his-based curcumin nanoformulations.
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