Pigeon egg white protein-based transparent durable hydrogel via monodisperse ionic surfactant-mediated protein condensation

• Published in: Scientific reports 2022-03, Vol.12 (1), p.4633-8, Article 4633
• Main Authors: Zhou, Xinlian, Chen, Zaozao, Nojima, Tatsuya
• Format: Article
• Language: English
• Subjects: 631/61/54/1754; 639/301/54/1754; 639/301/923/1027; Albumen; Animals; Columbidae; Compression; Compressive Strength; Egg Proteins; Gelation; Humanities and Social Sciences; Hydrogels; Mechanical properties; multidisciplinary; Optical properties; Proteins; Science; Science (multidisciplinary); Surface-Active Agents; Surfactants
• ISSN: 2045-2322; 2045-2322
• DOI: 10.1038/s41598-022-08375-x

The thermal gelation property of proteins is useful in creating protein-based materials. The gelation of protein solution often proceeds by the random aggregation of denatured proteins, and the protein-based gels are typically brittle or opaque, or both. Improvement in the mechanical and optical properties of protein-based materials are required for them to be practical and functional. This study investigated pigeon egg white, which is semitransparent in its thermally gelled state, as a protein source for creating hydrogel materials. The protein thermal gelation process was initiated from the orderly condensed state of proteins complexed with monodisperse ionic surfactants to suppress random aggregation. The resultant gel showed transparency in the visible light region and was not destroyed at 99% compression under 17.8 MPa compressive stress, 350-fold higher than the compressive fracture strength of typical boiled pigeon egg white. These results showed that durable transparent hydrogels could be fabricated by the rational combination of natural proteins and surfactants.