A comprehensive review of recent advances in silk sericin: Extraction approaches, structure, biochemical...

Silks are natural polymers that have been widely used for centuries. Silk consists of a filament core protein, termed fibroin, and a glue-like coating substance formed of sericin (SER) proteins. This protein is extracted from the silkworm cocoons (particularly Bombyx mori) and is mainly composed of amino acids like glycine, serine, aspartic acid, and threonine. Silk SER can be obtained using numerous methods, including enzymatic extraction, high-temperature, autoclaving, ethanol precipitation, cross-linking, and utilizing acidic, alkali, or neutral aqueous solutions. Given the versatility and outstanding properties of SER, it is widely fabricated to produce sponges, films, and hydrogels for further use in diverse biomedical applications. Hence, many authors reported that SER benefits cell proliferation, tissue engineering, and skin tissue restoration thanks to its moisturizing features, antioxidant and anti-inflammatory properties, and mitogenic effect on mammalian cells. Remarkably, SER is used in drug delivery depending on its chemical reactivity and pH-responsiveness. These unique features of SER enhance the bioactivity of drugs, facilitating the fabrication of biomedical materials at nano- and microscales, hydrogels, and conjugated molecules. This review thoroughly outlines the extraction techniques, biological properties, and respective biomedical applications of SER.