Isolation, purification and characterization of silk protein sericin from cocoon peduncles of tropical tasar silkworm, Antheraea mylitta |
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Authors: | Dash Rupesh Mukherjee Soumen Kundu S C |
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Affiliation: | Department of Biotechnology, Indian Institute of Technology, Kharagpur 721302, India |
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Abstract: | A high molecular weight water-soluble glue protein, sericin was identified in the cocoon peduncle (a strong thread connecting the cocoons to the branches of the tree with a ring) of the tropical tasar silkworm, Antheraea mylitta. The sericin was isolated by 8 M urea containing 1% sodium dodecyl sulfate and β-mercaptoethenol (2%) or by 1% sodium chloride. The protein was purified by gel filtration chromatography. In SDS-PAGE, a single band of approximately 200 kDa was detected both in non-reducing and reducing conditions. Amino acid analysis showed that the protein is enriched in glycine and serine. There is a slight difference observed in amino acid composition between the sericin from cocoon peduncle and cocoon of A. mylitta. Secondary structure estimation by circular dichroism spectrometry showed 36.7% β-sheets, 52.7% random coils, 10.6% turns and no helices. |
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Keywords: | Non-mulberry silkworm Peduncle sericin SDS-PAGE CD spectroscopy |
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