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1. Self‐healing efficiency of cinnamaldehyde‐crosslinked soy protein resins with elongated soy protein microcapsules

   https://doi.org/10.1002/app.55324  

   Yong, Vuthtyra; Netravali, Anil N (May 2024, Journal of Applied Polymer Science)

   Abstract Self‐healing green thermoset soy protein isolate (SPI) based resins, crosslinked with cinnamaldehyde (CA), were developed. Self‐healing was achieved using elongated microcapsules (MCs) as against spherical MCs that have been used in most earlier studies. MCs containing SPI solution as healant within poly(d,l‐lactide‐co‐glycolide) shells were prepared using Water‐in‐oil‐in‐water (w/o/w) emulsion solvent evaporation (ESE) technique. Process parameters such as sodium tripolyphosphate (STP) and poly(vinyl alcohol) (PVA) concentrations and stirring speed were optimized to obtain elongated MCs. The average aspect ratio of MCs was over four. SPI resins crosslinked with 10% CA (10%CA‐SPI) increased Young's modulus and fracture stress by 54% and 87%, respectively, compared with their noncrosslinked counterpart. The resins containing 15% elongated MCs (15%MC‐10%CA‐SPI) showed self‐healing efficiencies of over 42% in fracture stress and about 35% in toughness recovery, after 24 h of healing. Improvement in self‐healing can be attributed to the high aspect ratio of the MCs that increases the probability of MCs being in the path of the microcracks and releasing the healant. Elongated MCs also contain higher amount of healant than spherical ones of same diameter. Self‐healing resins and composites can not only help prevent their premature failure but also improve their performance as well as service life and safety. 

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2. Ice Recrystallization Inhibition Activity of Soy Protein Hydrolysates

   https://doi.org/10.1021/acs.jafc.2c08701  

   Fomich, Madison; Día, Vermont P; Premadasa, Uvinduni I; Doughty, Benjamin; Krishnan, Hari B; Wang, Tong (August 2023, Journal of Agricultural and Food Chemistry)
3. Soy protein processing impacts the ice recrystallization inhibition activity of protein hydrolysates

   https://doi.org/10.1002/sfp2.1038  

   Fomich, Madison; Dia, Vermont; Wang, Tong (September 2024, Sustainable Food Proteins)

   Abstract Soy protein hydrolysates have demonstrated moderate ice recrystallization inhibition (IRI) activity, but the properties of the unhydrolyzed protein contributing to this activity are not well known. The objective of this research was to identify the main protein processing factors important to the varying IRI activities observed. Three possible modification reactions were applied to soy protein isolate (SPI): the Maillard reaction that can occur in soy flour before protein isolation, heat denaturation of the fully defatted protein, and heat denaturation of the protein with the presence of residual lipid, mainly polar phospholipids. These modified proteins were hydrolyzed by Alcalase protease (for 2 min) to produce hydrolysates, which were characterized by HPLC and FTIR to investigate how molecular weight (MW) and changes in secondary structure relate to IRI activity. A multilinear regression with the parameters of modification type, surface hydrophobicity, secondary structure profile, and average MW of the hydrolysates was used to investigate their roles in reducing ice crystal size. It was discovered that polar lipids present in the soy hydrolysate samples and MW were the only significant factors (p < 0.05) for IRI activity of SPI hydrolysates which had an ice crystal size reduction from 22.0% to 36.7%. This study demonstrates for the first time a protein hydrolysate‐phospholipid interaction can produce IRI active molecules. 

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4. Ultrasound-assisted air-jet spinning of silk fibroin-soy protein nanofiber composite biomaterials

   https://doi.org/10.1016/j.ultsonch.2023.106341  

   Yang, Futian; Wang, Fang; Mazahreh, Janine; Hu, Xiao (March 2023, Ultrasonics Sonochemistry)
5. Characterization of soy protein hydrolysate and lecithin complex for its novel antifreeze activity

   https://doi.org/10.1016/j.foodhyd.2025.111389  

   Fomich, Madison; Dia, Vermont; Wang, Tong (November 2025, Food Hydrocolloids)