The Effect of Ultrasonication on the Gelation Velocity and Structure of Silk Fibroin


Article Preview

Silk fibroin hydrogels is an important morphous of biomaterial. As a natural protein collosol, purified native silk fibroin solution can be gelatinized under certain conditions. The main mechanism of the gelation is that the fibroin molecules turn into the β-sheet conformation from the random coils. This transformation of silk fibroin molecules would be influenced by various parameters such as the temperature, pH value, ion concentration and so on. In this paper, the effect of ultrasonication on the gelation velocity and structure of silk fibroin were discussed. It is believed that the cavitations caused by sonication could accelerate the process of gelation of silk fibroin. Our experiments demonstrated that the ultrasonic treatment could greatly reduce the silk fibroin gelation time, especially at a high sonication power exceeding 400W. The results of XRD, FTIR, and Raman spectra indicated that the ultrasonication had no significant effect on the final structure and composition of the silk fibroin gels except the acceleration for the molecular transition from random coil and α-structure to β-sheet conformation of silk fibroin. The SEM images showed freeze-dried fibroin gels close to the ultrasonication source had compact structure, while the structure was more loosening far away to the source.



Advanced Materials Research (Volumes 175-176)

Main Theme:

Edited by:

Lun Bai and Guo-Qiang Chen




Y. Y. Wang et al., "The Effect of Ultrasonication on the Gelation Velocity and Structure of Silk Fibroin", Advanced Materials Research, Vols. 175-176, pp. 143-148, 2011

Online since:

January 2011




[1] Altman GH, Diaz F, Jakuba C et al: Biomaterials, Vol. 24(2003), p.401.

[2] Jin HJ, Kaplan DL: Nature, Vol. 424(2003), p.1057.

[3] Horan RL, Antle K, Collette AL et al: Biomaterials, Vol. 26(2005), p.3385.

[4] Kim UJ, Park J, Kim HJ et al: Biomaterials, Vol. 26 (2005), p.2775.

[5] Ishida M, Asakura T, Yokoi M et al: Macromole cules, Vol. 23(1990), p.88.

[6] Nazarov R, Jin HJ, Kaplan DL: Biomacromolecules, Vol. 5(2004), p.718.

[7] Jin HJ, Park J, Valluzzi R et al: Biomacromolecules, Vol. 5(2004), p.711.

[8] Jin HJ, Fridrikh SV, Rutledge GC et al: Biomacromolecules, Vol. 3(2002), p.1233.

[9] Hino T, Tanimoto M, Shimabayashi S: Colloid Interface Sci, Vol. 266(2003), p.68.

[10] Minour N, Tsukada M, Nagura M: Biomaterials, Vol. 11(1990), p.430.

[11] Opdahl A, Kim SH, Koffas TS et al: J Biomed Mater Res, Vol. 67(2003), p.350.

[12] Nowak AP, Breedveld V, Pakstis L. et al: Nature, Vol. 417(2002), p.424.

[13] Wang H, Zhang Y, Shao H, Hu X: Int J Biol Macromol, Vol. 36(2005), p.66.

[14] Kim UJ, Park J, Li C et al: Biomacromolecules, Vol. 5(2004), p.786.

[15] Matsumoto A, Chen J, Collette AL et al: J Phys Chem B, Vol. 110(2006), p.21630.

[16] Fini M, Motta A, Torricelli P et al: Biomaterials, Vol. 26(2005), p.3527.

[17] Motta A, Migliliaresi C, Faccioni F et al: J Biomater Sci Polym Edn, Vol. 15(2004), p.851.

[18] X. Wang, J.A. Kluge, G.G. Leisk et al: Biomaterials, Vol. 29(2008), p.1054.

[19] M Li, S Lu, Z Wu et al: J. Appl. Polym. Sci, Vol. 79(2001), p.2185.

[20] Paulusse JMJ, Sijbesma RP: J Polym Sci -Polym Chem, Vol. 44(2006), p.5445.

[21] Kemmere MF, Kuijpers MWA et al: Macromol Mater Eng, Vol. 290(2005), p.302.

[22] Shimizu M. Sanshi Shikenjo: Houkoku Vol. 10(1941), p.475.

[23] Hirabayashi K, Ishikava H: Sen-i Gakkaishi Vol. 23(1967); p.538.

[24] M Li, Z Wu, S Lu et al: J. Dong Hua University (Nature Science Edition), Vol. 27(2001), p.12.

[25] M Tsukada, Y Gotohet al: J. Polym. Sci Part A: Polymer Chemistry, Vol. 32(1994), p.961.

[26] H Yoshimizu, T Asakura: J. Appl. Polym. Sci, Vol. 40(1990), p.1745.

[27] P. R. Carey, P. Fast, H. Kaplan et al: Vol. 872(1986), p.169.

[28] E. Li-Chan, S. Nakai and M. Hirotsuka. Edited by R. Y. Yada, R. L. Jackman and J. L. Smith, Chapman & Hall, (1994), p.163.