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A novel method for dissolution and stabilization of non‐mulberry silk gland protein fibroin using anionic surfactant sodium dodecyl sulfate
Author(s) -
Mandal Biman B.,
Kundu S. C.
Publication year - 2007
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.21699
Subject(s) - fibroin , sodium dodecyl sulfate , pulmonary surfactant , biopolymer , chemistry , dissolution , circular dichroism , chemical engineering , micelle , silk , gel electrophoresis , polymer chemistry , nuclear chemistry , biophysics , chromatography , polymer , crystallography , biochemistry , organic chemistry , materials science , aqueous solution , biology , composite material , engineering
The importance of silk protein has increased because of its potential use as a natural biopolymer for tissue engineering and biomedical applications. In this report we show a novel and ecofriendly method for dissolution of gland silk protein fibroin. Non‐mulberry silk fibroin from mature fifth instar larvae of Antheraea mylitta was found to be optimally soluble in 1% (w/v) anionic surfactant sodium dodecyl sulfate (SDS). Regenerated fibroin showed distinct bands of approximately 395 and 197 kDa on electrophoresis in non‐reducing and reducing conditions, respectively. Enhanced fibroin dissolution via internalization of hydrophobic amino groups inside a hydrophilic amino acid core in the form of micelles was observed. Prolonged storage stability without gelation of SDS‐extracted fibroin was seen. Atomic force microscopy showed micellar aggregation with mean micellar aggregation size of 8 nm. Circular dichroism spectroscopy revealed predominantly helical conformation due to surfactant addition with internal protein conformational changes as revealed by fluorescence spectroscopic studies. Biotechnol. Bioeng. 2008;99: 1482–1489. © 2007 Wiley Periodicals, Inc.