Effect of .ALPHA.-chymotrypsin on the structure of silk fibroin.

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  • α‐キモトリプシンを作用させた絹フィブロインの構造
  • アルファ キモトリプシン オ サヨウサセタ キヌ フィブロイシ ノ コウゾウ

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Abstract

Structure of the chymotrypsin-resistant fraction from regenerated (solubilized) silk fibroin (Fli·cp) and native silk fibroin (FN·cp) was studied by infrared spectroscopy, x-ray diffractometry, scanning electron microscopy and DSC measurement.<br>On the basis of the infrared spectra and x-ray diffraction micrographs, it was found that chymotrypsin-resistant Fli·cp and FN·cp exhibited the silks and silk I crystalline form, respectively, suggesting that the crystalline structure of silk fibroin differed markedly as a result of the change of the specimen's preparation. The thermal decomposition temperature of Fli·cp shifted to a higher temperature compared to that of the coagulated silk fibroin with a silk II crystalline form, depending largely on the presence of highly organized crystallite and the removal of the random coil region resulting from the action of chymotrypsin. Scanning electron micrographs of Fli·cp revealed a granular form (0.3μm in diameter), differing significantly from that for FN·cp.

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