PHYSIO-CHEMICAL & MOLECULAR CHARACTERIZATION OF SERICIN DERIVED FROM TASAR AND MULBERRY SILK

Abstract

This study investigates the physio-chemical and molecular characteristics of sericin proteins derived from Tasar (Antheraea mylitta) and Mulberry (Bombyx mori) silk. Sericin, a silk protein with applications across textiles, cosmetics, and biomedical industries, is valued for its biocompatibility, antioxidant properties, and ease of extraction. However, the physio-chemical properties of sericin can vary significantly depending on the silk source, affecting its industrial potential. Through spectroscopic (FTIR, UV-Vis), chromatographic (HPLC), and thermal (DSC, TGA) analyses, this research compares Tasar and Mulberry sericin in terms of molecular weight, structural stability, solubility, and thermal behavior. Molecular characterization is further conducted to evaluate amino acid composition and structural variances between the two types. Results indicate unique properties in Tasar sericin, such as enhanced thermal stability and distinct molecular structures, which could extend its functionality in specific applications. This comparative analysis underscores the value of detailed sericin characterization for optimizing its use in diverse applications.