TY - JOUR
T1 - Silk-Soy Alloy Materials
T2 - Influence of Silk Types (Mori, Thai, Muga, Tussah, and Eri) on the Structure, Properties, and Functionality of Insect–Plant Protein Blends (II)
AU - Poluri, Nagireddy
AU - Gough, Christopher R.
AU - Perrotta, Joseph
AU - Pinto, Joseph
AU - Cohen, Maxwell
AU - Sanderlin, Steven
AU - Velardo, Christopher
AU - Barca, Anthony
AU - Hu, Xiao
N1 - Publisher Copyright:
© 2025 by the authors.
PY - 2025/5
Y1 - 2025/5
N2 - Natural proteins present a sustainable and biocompatible alternative to conventional fossil fuel-derived plastics, with versatile applications in fields ranging from medicine to food packaging. Extending our previous research on silk–corn zein composites, this study utilizes soy protein—another plant protein extensively employed within biomedical applications—in conjunction with silk fibroin proteins extracted from a variety of domestic (Mori and Thai) and wild (Muga, Tussah, and Eri) silkworm species. By combining these proteins in varying ratios (0%, 10%, 25%, 50%, 75%, 90%, and 100%), silk–soy films were successfully fabricated with high miscibility. The structural and thermal stability of these films was confirmed through various characterization techniques, including Fourier transform infrared spectroscopy (FTIR), differential scanning calorimetry (DSC), and scanning electron microscopy (SEM). Structural refinements were then achieved through post-water annealing treatments. After annealing, it was observed that when soy protein was introduced into both types of silk, the silks exhibited a greater amount of intermolecular and intramolecular β-sheet content. This phenomenon can be attributed to soy’s intrinsic ability to self-assemble into β-sheets through electrostatic and hydrophobic interactions, which also improved the overall thermal stability and morphology of the composite films. The unique self-assembling properties of soy and its ability to promote β-sheet formation facilitate the customization of the silk source and the soy-to-silk ratio. This adaptability establishes protein-based thin films as a versatile and sustainable option for diverse applications in fields such as medicine, tissue engineering, food packaging, and beyond.
AB - Natural proteins present a sustainable and biocompatible alternative to conventional fossil fuel-derived plastics, with versatile applications in fields ranging from medicine to food packaging. Extending our previous research on silk–corn zein composites, this study utilizes soy protein—another plant protein extensively employed within biomedical applications—in conjunction with silk fibroin proteins extracted from a variety of domestic (Mori and Thai) and wild (Muga, Tussah, and Eri) silkworm species. By combining these proteins in varying ratios (0%, 10%, 25%, 50%, 75%, 90%, and 100%), silk–soy films were successfully fabricated with high miscibility. The structural and thermal stability of these films was confirmed through various characterization techniques, including Fourier transform infrared spectroscopy (FTIR), differential scanning calorimetry (DSC), and scanning electron microscopy (SEM). Structural refinements were then achieved through post-water annealing treatments. After annealing, it was observed that when soy protein was introduced into both types of silk, the silks exhibited a greater amount of intermolecular and intramolecular β-sheet content. This phenomenon can be attributed to soy’s intrinsic ability to self-assemble into β-sheets through electrostatic and hydrophobic interactions, which also improved the overall thermal stability and morphology of the composite films. The unique self-assembling properties of soy and its ability to promote β-sheet formation facilitate the customization of the silk source and the soy-to-silk ratio. This adaptability establishes protein-based thin films as a versatile and sustainable option for diverse applications in fields such as medicine, tissue engineering, food packaging, and beyond.
UR - https://www.scopus.com/pages/publications/105006706649
UR - https://www.scopus.com/inward/citedby.url?scp=105006706649&partnerID=8YFLogxK
U2 - 10.3390/ijms26104563
DO - 10.3390/ijms26104563
M3 - Article
C2 - 40429708
AN - SCOPUS:105006706649
SN - 1661-6596
VL - 26
JO - International Journal of Molecular Sciences
JF - International Journal of Molecular Sciences
IS - 10
M1 - 4563
ER -