Amyloid aggregation in mixed whey proteins
Year: 2025
Authors: Venturi S., Rossi B., Matroodi F., Torre R., Lapini A., Foggi P., Di Michele A., Sassi P., Paolantoni M., Catalini S.
Autors Affiliation: Univ Firenze, European Lab Nonlinear Spect, Via Nello Carrara 1, I-50019 Sesto Fiorentino, Italy; Elettra Sincrotrone Trieste, SS 114 Km 163-5, I-34149 Trieste, Italy; Shahid Chamran Univ Ahvaz, Dept Phys, Ahvaz, Iran; Univ Firenze, Dipartimento Fis & Astron, Via G Sansone 1, I-50019 Sesto Fiorentino, Italy; Univ Parma, Dipartimento Sci Chim Vita & Sostenibil Ambientale, Parco Area Sci 17-A, I-43124 Parma, Italy; Univ Perugia, Dipartimento Chim Biol & Biotecnol, Via Elce Sotto 8, I-06123 Perugia, Italy; CNR, CNR INO, Ist Nazl Ottica, Largo Fermi 6, I-50125 Florence, Italy; Univ Perugia, Dipartimento Fis & Geol, Via Pascoli, I-06123 Perugia, Italy.
Abstract: The fundamental principles behind the complexity of protein assembly, especially in mixed protein systems and crowded environments, remain elusive. This study provides molecular, structural, and viscoelastic insights into the aggregation and gelation processes in aqueous solutions of pure and mixed beta-lactoglobulin and albumin whey proteins. To better understand protein aggregation in complex systems, we used a multi-technique approach that spans from molecular to macroscopic length scales. Our results show that, under low pH and heat denaturation, beta-lactoglobulin tends to form ordered amyloid-type aggregates, while bovine serum albumin forms non-amyloid aggregates. In crowded environments, all protein solutions tested develop composite gel networks with distinct molecular origins. Here the ability to control the amyloid aggregate content, which has a substantial effect on the structural and viscoelastic properties of these composite gels, has been demonstrated. Gel structure and viscosity are crucial parameters to control for the food industry, as they play a key role in determining the softness and texture of food products.
Journal/Review: FOOD HYDROCOLLOIDS
Volume: 161 Pages from: 110863-1 to: 110863-14
More Information: We acknowledge Elettra Sincrotrone Trieste for providing access to its synchrotron radiation facilities and for financial support under the SUI internal project (proposal number 20220424) . The authors acknowledge the CERIC-ERIC Consortium for the access to experimental facilities and financial support (proposal number 20227195) . The authors are grateful to Heinz for the assistance on SAXS beamline. S.C. thank the research project FSE-REACT EU financed by National Social Fund-National Operative Research Program and Innovation 2014-2020 (D.M. 1062/2021) , personal Grant number 23-G-15445-3. P.F., A.D.M., P.S., M.P., and S.C. thank the European Union NextGenerationEU project under the Italian Ministry of University and Research (MUR) National Innovation Ecosystem grant ECS00000041-VITALITY-CUP: J97G22000170005 and B43C22000470005. This research was funded by Next Generation EU Programme: project PRIN-2022JWAF7Y and I-PHOQS Infrastructure [IR0000016, ID D2B8D520, CUP B53C22001750006] ; project CNR-FOE-LENS-2023 and Horizon 2020 EU Programme project Laserlab-Europe n. 871124.KeyWords: whey proteins aggregation; protein-based hydrogels; beta-lactoglobulin; albumin; UV resonance Raman; FTIR; SAXS; HD-TGDOI: 10.1016/j.foodhyd.2024.110863
