Dissolution and characterization of regenerated Antheraea pernyi silk fibroin
β Scribed by Haeyong Kweon; Young Hwan Park
- Publisher
- John Wiley and Sons
- Year
- 2001
- Tongue
- English
- Weight
- 256 KB
- Volume
- 82
- Category
- Article
- ISSN
- 0021-8995
- DOI
- 10.1002/app.1901
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β¦ Synopsis
Abstract
Dissolution of Antheraea pernyi silk fiber was carried out in a calcium nitrate solution with various dissolving conditions. The solubility was significantly dependent on the concentration of calcium nitrate, dissolving temperature, and time. The proper conditions of dissolution were found as 7__M__ calcium nitrate, 100Β°C temperature, and 3 h dissolving time. The aqueous solution of A. pernyi silk fibroin was composed of a mixture of polypeptides with several molecular weights above 14 kDa. FTIR and XRD showed that regenerated A. pernyi silk fibroin was composed of an Ξ±βhelix as well as a randomβcoil conformation while silk fiber had a traditional Ξ²βsheet structure. The endoβexo transition in the temperature ranges of 228β232Β°C also supports these conformations of regenerated silk fibroin film. TGA and DTG curves showed that the thermal decomposition of regenerated A. pernyi silk fibroin proceeded by three steps, not dependent on the conformation. The mechanical damping peaks (tan Ξ΄) appeared about 227Β°C with a minor shoulder maximum about 240Β°C, which were somewhat lower than those of tussah silk fiber. Β© 2001 John Wiley & Sons, Inc. J Appl Polym Sci 82: 750β758, 2001
π SIMILAR VOLUMES
The regenerated Antheraea pernyi silk fibroin films were prepared from calcium nitrate solution and crystallized with aqueous methanol solution. The structural and conformational changes were investigated by the X-ray diffraction method and infrared spectroscopy upon methanol treatment. The concentr
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Bombyx mori silk fibroin from the silkworm was found to be soluble in a calcium nitrate-methanol system. Fibroin dissolves in 75% w/v Ca(NO 3 ) 2 /MeOH solution at a temperature of 67ΠC. The viscometric behavior of the fibroin-salt solution was analyzed and the fibroin's secondary structures were de
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