Bioplastic films were developed through the valorization of waste proteins from black soldier flies (BSFs) and sericin. Following proteomic characterization, the films were prepared and their properties were correlated with the structure of the proteins. Higher molecular mass and transitions towards β-sheet architectures were found to significantly improve mechanical performance. Protocols specific to the proteins were developed for amyloid fibrillization, which further enhanced the properties of the films in both pure protein systems and blends with biodegradable polymers. Lyophilised amyloid-containing proteins were also used as nanofillers to reinforce biodegradable polymer matrices. Overall, amyloid fibrillization proved to be an effective strategy for producing protein-based materials with properties comparable to those of commercially available biopolymers.

Structural control and amyloid reinforcement of waste-derived protein films

M. Colombo;E. Testa;E. Fasoli;D. Gentile;V. Barbera;M. Galimberti
2026-01-01

Abstract

Bioplastic films were developed through the valorization of waste proteins from black soldier flies (BSFs) and sericin. Following proteomic characterization, the films were prepared and their properties were correlated with the structure of the proteins. Higher molecular mass and transitions towards β-sheet architectures were found to significantly improve mechanical performance. Protocols specific to the proteins were developed for amyloid fibrillization, which further enhanced the properties of the films in both pure protein systems and blends with biodegradable polymers. Lyophilised amyloid-containing proteins were also used as nanofillers to reinforce biodegradable polymer matrices. Overall, amyloid fibrillization proved to be an effective strategy for producing protein-based materials with properties comparable to those of commercially available biopolymers.
2026
Structural control and amyloid reinforcement of waste-derived protein films
waste, proteins, amyloid fibrils, films, bioplastic
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11311/1325556
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