低温又は水繰が可能な蚕品種による繭層セリシンの構造特性

概要

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The physical properties of silk sericin expected from cocoon shells of silkworm varieties with different values of sericin solubility were investigated by polyacrylamide gel electrophoresis, differential scanning calorimetry (DSC), X-ray diffraction and infrared spectroscopy (IR). The electrophoretic pattern of the silk sericin components extracted from the cocoon shell at 38°C was similar with the exception of the sericin band corresponding to S-2 (S-2′). DSC curves of silk sericin showed on endothermic peak at around 225°C which was attributed to thermal decomposition. The temperature for decomposition did not change regardless of the differences in the silkworm races. The crystalline structure of the components was similar to each other. Infrared spectra demonstrated that silk sericin displays a molecular conformation characterized by a random coil and β structure.
日本蠶絲學會の論文