Research On The Structural Transformation Of Regenerated Bombyx Mori Silk Fibroin

We focused on the structural transformation of silk fibroin proteins at the air-water interface. By means of X-ray diffraction, FT-IR spectroscopy, Raman spectroscopy and Scanning electron microscopy, we analyzed the structure of silk films which were formed at the air-water interface by the induction of air, and the results showed that air can drive the structural transformation of silk fibroin protein from random coil toα-form orβ-form.The effect of Glycol,Glycerin,Polyethylene Glyco(lMol.Wt. 400),Polyethylene Glyco(lMol.Wt. 600) on the structural transformation of silk fibroin protein was studied. When the addition of polyalcohol reached 100%, the gelation of silk fibroin solution would be delayed, but when the addition raised 300% and more, the gelation of silk fibroin solution would be accelerated. The more the addition, the lower the crystallinity of the silk fibroin hydrogels. Adding more polyalcohol(such as 900%) will obstruct the formation ofβ-sheet.The effect of superaudible on the structural transformation of silk fibroin protein was studied. We analyzed the structure of silk fibroin hydrogels and the results showed that superaudible can accelerate the gelation of silk fibroin solution, because superaudible can accelerate the structural transformation of silk fibroin protein from random coil toβ-sheet. Hyperacoustic power does not affect the condensed structure and crystallinity of silk fibroin hydrogels obviously.The effect of shearing force on the structural transformation of silk fibroin protein was studied. The results showed that shearing force can accelerate the gelation of silk fibroin solution, because shearing force can accelerate the formation ofβ-form. After shearing , the crystallinity of silk fibroin hydrogel was improved. The shearing rate of 150r/min is excellent for the acceleration of gelation and crystallinity of silk fibroin hydrogel.