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Updated: Jun 2, 2026

Synthesis of an Intein-mediated Artificial Protein Hydrogel
Published on: January 27, 2014
Double-aimed superstructure: delivering nutritional divalent cations as whey protein isolate fibril mediator to
Zahra Kazemi-Taskooh1, Mehdi Varidi1
1Department of Food Science and Technology, Faculty of Agriculture, Ferdowsi University of Mashhad, Azadi Sq., Mashhad, Khorasan Razavi, P.O. Box 9177948944, Iran.
Abstract:
The physicochemically characterized divalent cation-driven whey protein isolate (WPI) fibrils were assessed by interfacial viewpoint, then the corresponding ultrastable HIPPEs containing nutritional cations were characterized. The amyloids mediated the interfacial interactions with in-plane bending, producing a firm elastic temperature-independent structure. The multi-core microstructure of Fe2+-mediated fibrils with high bundling minimized the textural properties and complex viscosity (105-112 mPa.s) with reduced elastic portion. The Ca2+- and Mg2+-assisted fibrils less influenced by hydrophobic forces had the minimum oil loss (1.1, 0.59%). Multi-layered microstructure of Zn2+-driven fibrils reduced fibril-water interactions. The semi-flexible zigzag-shaped interwined microstructure of Ca2+-driven fibrils greatly stabilized the HIPPE at high frequencies (100 Hz). The random coils reduced the fibril ability to hold water, reducing firmness. The oxygen permeation respectively increased and decreased by heavy components and polygonal shape of the oil droplets. Larger ionic radii increased electrophoretic mobility of fibrils, reducing the droplet size of HIPPEs by Coulomb repulsions.
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