Dissolution and regeneration of non-mulberry Eriogyna Pyretorum silk fibroin

Protein-based materials have been actively pursued as biomaterials because of their nontoxicity, biocompatibility and biodegradability. In this work, we demonstrated the potential of Eriogyna pyretorum silk fibroin (ESF), a non-mulberry silk protein, as biomaterials. The degummed ESF fibers could be dissolved completely by Ca(NO 3 ) 2 /H 2 O/C 2 H 5 OH solution to produce regenerated ESF. The solubility was strongly dependent on the addition of C 2 H 5 OH, heating temperature and dissolving time. α -helix and random coil are main molecular conformation in aqueous ESF solution. The sol–gel transition behavior of regenerated ESF was also studied, indicating that the conformational transition of regenerated ESF from random coil/ α -helix to β -sheet during gelation. Especially, ESF showed more rapid gelation than mulberry silk fibroin (BSF). Consequently, the gelation rate of BSF could be controlled ranging from tens of minutes to days by changing the ESF ratio, providing useful options for the fabrication of silk hydrogels. Water-stable regenerated ESF film could be achieved by using aqueous ethanol to induce structural transition. Tensile tests showed that the ESF films have a dry strength of approximate 31.0 MPa and a wet strength of approximate 3.3 MPa. This study provides new opportunities as an alternative natural protein material for biomedical applications.