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Optimization of the silk scaffold sericin removal process for retention of silk fibroin protein structure and mechanical properties

Abstract

In the process of removing sericin (degumming) from a raw silk scaffold, the fibroin structural integrity is often challenged, leading to mechanical depreciation. This study aims to identify the factors and conditions contributing to fibroin degradation during alkaline degumming and to perform an optimization study of the parameters involved to achieve preservation of fibroin structure and properties. The methodology involves degumming knitted silk scaffolds for various durations (5-90 min) and temperatures (60-100 {sup 0}C). Mechanical agitation and use of the refreshed solution during degumming are included to investigate how these factors contribute to degumming efficiency and fibroin preservation. Characterizations of silk fibroin morphology, mechanical properties and protein components are determined by scanning electron microscopy (SEM), single fiber tensile tests and gel electrophoresis (SDS-PAGE), respectively. Sericin removal is ascertained via SEM imaging and a protein fractionation method involving SDS-PAGE. The results show that fibroin fibrillation, leading to reduced mechanical integrity, is mainly caused by prolonged degumming duration. Through a series of optimization, knitted scaffolds are observed to be optimally degummed and experience negligible mechanical and structural degradation when subjected to alkaline degumming with mechanical agitation for 30 min at 100 {sup 0}C.
Authors:
Teh, Thomas K H; Toh, Siew-Lok; Goh, James C H, E-mail: dosgohj@nus.edu.s, E-mail: dostkh@nus.edu.s, E-mail: bietohsl@nus.edu.s [1] 
  1. Division of Bioengineering, National University of Singapore (Singapore)
Publication Date:
Jun 01, 2010
Product Type:
Journal Article
Resource Relation:
Journal Name: Biomedical Materials (Bristol. Online); Journal Volume: 5; Journal Issue: 3; Other Information: DOI: 10.1088/1748-6041/5/3/035008; PII: S1748-6041(10)43237-4
Subject:
60 APPLIED LIFE SCIENCES; ELECTROPHORESIS; FRACTIONATION; GELS; MECHANICAL PROPERTIES; OPTIMIZATION; PROTEIN STRUCTURE; PROTEINS; REMOVAL; SCANNING ELECTRON MICROSCOPY; SILKWORM; ANIMALS; ARTHROPODS; COLLOIDS; DISPERSIONS; ELECTRON MICROSCOPY; INSECTS; INVERTEBRATES; LEPIDOPTERA; MICROSCOPY; MOTHS; ORGANIC COMPOUNDS; SEPARATION PROCESSES
OSTI ID:
21455810
Country of Origin:
United Kingdom
Language:
English
Other Identifying Numbers:
Journal ID: ISSN 1748-605X; TRN: GB10I0692050917
Availability:
Available from http://dx.doi.org/10.1088/1748-6041/5/3/035008
Submitting Site:
GBN
Size:
12 pages
Announcement Date:
Jul 21, 2011

Citation Formats

Teh, Thomas K H, Toh, Siew-Lok, and Goh, James C H, E-mail: dosgohj@nus.edu.s, E-mail: dostkh@nus.edu.s, E-mail: bietohsl@nus.edu.s. Optimization of the silk scaffold sericin removal process for retention of silk fibroin protein structure and mechanical properties. United Kingdom: N. p., 2010. Web. doi:10.1088/1748-6041/5/3/035008.
Teh, Thomas K H, Toh, Siew-Lok, & Goh, James C H, E-mail: dosgohj@nus.edu.s, E-mail: dostkh@nus.edu.s, E-mail: bietohsl@nus.edu.s. Optimization of the silk scaffold sericin removal process for retention of silk fibroin protein structure and mechanical properties. United Kingdom. doi:10.1088/1748-6041/5/3/035008.
Teh, Thomas K H, Toh, Siew-Lok, and Goh, James C H, E-mail: dosgohj@nus.edu.s, E-mail: dostkh@nus.edu.s, E-mail: bietohsl@nus.edu.s. 2010. "Optimization of the silk scaffold sericin removal process for retention of silk fibroin protein structure and mechanical properties." United Kingdom. doi:10.1088/1748-6041/5/3/035008. https://www.osti.gov/servlets/purl/10.1088/1748-6041/5/3/035008.
@misc{etde_21455810,
title = {Optimization of the silk scaffold sericin removal process for retention of silk fibroin protein structure and mechanical properties}
author = {Teh, Thomas K H, Toh, Siew-Lok, and Goh, James C H, E-mail: dosgohj@nus.edu.s, E-mail: dostkh@nus.edu.s, E-mail: bietohsl@nus.edu.s}
abstractNote = {In the process of removing sericin (degumming) from a raw silk scaffold, the fibroin structural integrity is often challenged, leading to mechanical depreciation. This study aims to identify the factors and conditions contributing to fibroin degradation during alkaline degumming and to perform an optimization study of the parameters involved to achieve preservation of fibroin structure and properties. The methodology involves degumming knitted silk scaffolds for various durations (5-90 min) and temperatures (60-100 {sup 0}C). Mechanical agitation and use of the refreshed solution during degumming are included to investigate how these factors contribute to degumming efficiency and fibroin preservation. Characterizations of silk fibroin morphology, mechanical properties and protein components are determined by scanning electron microscopy (SEM), single fiber tensile tests and gel electrophoresis (SDS-PAGE), respectively. Sericin removal is ascertained via SEM imaging and a protein fractionation method involving SDS-PAGE. The results show that fibroin fibrillation, leading to reduced mechanical integrity, is mainly caused by prolonged degumming duration. Through a series of optimization, knitted scaffolds are observed to be optimally degummed and experience negligible mechanical and structural degradation when subjected to alkaline degumming with mechanical agitation for 30 min at 100 {sup 0}C.}
doi = {10.1088/1748-6041/5/3/035008}
journal = {Biomedical Materials (Bristol. Online)}
issue = {3}
volume = {5}
place = {United Kingdom}
year = {2010}
month = {Jun}
}