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<p>The ability of proteins to self-assemble into ordered structures is a key feature in nature to produce highly functional biomacromolecules. This spontaneous organization of polypeptides can be utilized in technology to develop environment-friendly, protein-based bioplastic films with enhanced properties from various proteins. This study focuses on tailoring the mechanical and functional properties of solvent-cast films by pH value manipulation (10, 7, 2), acetic acid treatment, and ultrasonication of heated (85&#xa0;°C, 30&#xa0;min) solutions of lupin protein isolate (LPI). A combination of acetic acid and ultrasonic treatment yielded LPI films that exhibited increased tensile strengths of 6.8 ± 0.4&#xa0;MPa, Young’s moduli of 270 ± 18&#xa0;MPa, and works of fracture of 4.4 ± 0.5&#xa0;MPa, together with high optical transmissions and water stability compared to the other investigated films. Structural investigations indicated the formation of self-assembled protein nanostructures with an increased fraction of β-sheets. Small-angle X-ray scattering investigations were performed to gain insights into the nanostructural evolution of protein aggregates from LPI during the evaporation of water.</p>

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Tailoring the Mechanical and Functional Properties of Lupin Protein Films by pH Manipulation, Acetic Acid, and Ultrasonic Treatment

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年7月17日

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  • Maximilian Maidl,
  • Daniel Van Opdenbosch,
  • Cordt Zollfrank

摘要

The ability of proteins to self-assemble into ordered structures is a key feature in nature to produce highly functional biomacromolecules. This spontaneous organization of polypeptides can be utilized in technology to develop environment-friendly, protein-based bioplastic films with enhanced properties from various proteins. This study focuses on tailoring the mechanical and functional properties of solvent-cast films by pH value manipulation (10, 7, 2), acetic acid treatment, and ultrasonication of heated (85 °C, 30 min) solutions of lupin protein isolate (LPI). A combination of acetic acid and ultrasonic treatment yielded LPI films that exhibited increased tensile strengths of 6.8 ± 0.4 MPa, Young’s moduli of 270 ± 18 MPa, and works of fracture of 4.4 ± 0.5 MPa, together with high optical transmissions and water stability compared to the other investigated films. Structural investigations indicated the formation of self-assembled protein nanostructures with an increased fraction of β-sheets. Small-angle X-ray scattering investigations were performed to gain insights into the nanostructural evolution of protein aggregates from LPI during the evaporation of water.