Bombyx mori, the domesticated mulberry silkworm, lepidopteran molecular model and the most significant economic insect. It is emerging as a great molecular genetic resource for tackling biological challenges. During the final stage of larval development, the silkworm B. mori produces massive quantities of silk proteins. These proteins are stored in the middle silk gland and expelled through the spinneret at the end of the fifth instar. Silk fibroin and sericin are the two prime silk proteins in the silk cocoons. Silk fibroin is a fibrous protein composed up of heavy chain (H), light chain (L), and glycoprotein linked by disulfide bonds, as well as sericin, a macromolecular protein that acts as an adhesive substance to combine fibroin for the production of cocoons of silkworm B. mori. A brief synopsis of sericin is given in this review. The structure, content, solubility, genetics, and characteristics of silk sericin are the main topics of this review. Large amounts of sericin, a silk protein, are often discarded by the textile and sericulture industries during the degumming process of production silk from silk cocoons. Because sericin is highly hydrophilic and confers useful biological and biocompatible properties like antibacterial, antioxidant, anticancer, and anti-tyrosinase properties, it can be investigated for its application. Aspartic acid, glycine, and serine are among the beneficial amino acids found in sericin, which is derived from silk cocoons. The creation of films, coatings, and packaging materials has shown the effectiveness of using sericin in combination with other biomaterials.