tSilk proteins of silkworms are chiefly composed of core fibroin protein and glycoprotein sericin that gluesfibroin. Unique mechanical properties, cyto-compatibility and controllable biodegradability facilitate theuse of fibroin in biomedical applications. Sericin serves as additive in cosmetic and food industries, asmitotic factor in cell culture media, anti-cancerous drug, anticoagulant and as biocompatible coating. Forall these uses; aqueous solutions of silk proteins are preferred. Therefore, an accurate understanding ofextraction procedure of silk proteins from their sources is critical. A number of protocols exist, amongstwhich it is required to settle a precise and easy one with desired yield and least down-stream processing.Here, we report extraction of proteins employing methods mentioned in literature using cocoons ofmulberry and nonmulberry silks. This study reveals sodium carbonate salt-boiling system is the mostefficient sericin extraction procedure for all silk variants. Lithium bromide is observed as the effectivefibroin dissolution system for mulberry silk cocoons; whereas heterogeneous species-dependent resultis obtained in case of nonmulberry species. We further show the effect of common post processing onnanoscale morphology of mulberry silk fibroin films. This knowledge eases the adoption and fabricationof silk biomaterials in devices and therapeutic delivery systems