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sericin is a group of soluble glycoproteins expressed in the middle silk gland of Bombyx mori. Several genes have been identified in Bombyx mori and other species (Craig and Riekel, 2002). These proteins cover the surface of fibroin, the silk filament core protein, in the cocoon filament.

Sericin S (sericin small), a preparation with a molecular weight of 5-100 kDa has been used as a cell culture supplement and accelerates cell proliferation of hybridoma cells in various serum-free media. Sericin S also induces the proliferation of CTLL-2 cells under IL2 starvation conditions (Terada et al, 2005).

Takahashi et al (2005) have reported that Sericin hydrolysate protects cultured Sf9 insect cells from death caused by serum deprivation. The activity depends on the repeats of 38 amino acids, and a partial peptide from the 38 residues, SGGSSTYGYS, also inhibits serum-deprivation death. Tsubouchi et al (2005) have reported that sericin M, the main sericin component of about 400 kDa enhances attachment of cultured human skin fibroblasts, raising the living cell number after 72 hrs to 250 % of the no-sericin control.

Wound healing in sericin-treated wounds is accelerated and proceeds with less inflammatory reactions than in untreated wounds (Aramwit and Sangcakul, 2007).

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