Isolation, purification and characterization of silk protein sericin from cocoon peduncles of tropical tasar silkworm, Antheraea mylitta

被引：71

作者：

Dash, Rupesh ^{[1
]}

Mukherjee, Soumen ^{[1
]}

Kundu, S. C. ^{[1
]}

机构：

[1] Indian Inst Technol, Dept Biotechnol, Kharagpur 721302, W Bengal, India

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2006年 / 38卷 / 3-5期

关键词：

non-mulberry silkworm; peduncle sericin; SDS-PAGE; CID spectroscopy;

D O I：

10.1016/j.ijbiomac.2006.03.001

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 beta-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% beta-sheets, 52.7% random coils, 10.6% turns and no helices. (c) 2006 Elsevier B.V. All rights reserved.

引用

页码：255 / 258

页数：4

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