Abstract
The present study investigates the properties of sericin extracted from tasar silk fiber waste (TSFW). The surface morphology of TSFW was observed by scanning electron microscope (SEM). SEM images revealed the removal of residual sericin over the surface of TSFW. The molecular weight distribution of sericin was examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The results suggested that TSFW sericin represented a family of proteins with wide-ranging molecular weight distribution (11–245 kDa). Structural determination by FTIR revealed the presence of both α-helical and β-sheet structures. The colour was studied by colorimeter indicating less brightness, more red and yellow colour intensities. The carbon: nitrogen ratio (C:N) was studied by CHNS element analyzer and the ratio is 5.15-7.85. Thermal properties of TSFW sericin have been studied by thermogravimetric analysis (TGA) method. TGA curve showed higher thermal stability and variable degradation profiles. Furthermore, TSFW sericin contains 17 amino acids where serine, aspartic acid and glycine are the more significant compounds (54.34–60.49%). In addition, sericin was found to inhibit tyrosinase, elastase and glutathione-S-transferase activity, and had apparent radical scavenging impacts on 2.2‑diphenyl‑1‑picryl‑hydrazil (DPPH), hydrogen peroxide and inhibition of lipid peroxidation. Result suggested that TSFW sericins might be a valuable ingredient for cosmoceutical products.
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More From: International Journal of Biological Macromolecules
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