Silk remarkable mechanical properties, comparative biocompatibility, tunable degradation rates "in vitro" and "in vivo", the ease to load cellular growth factors (for example, BMP-2), and the ability to be processed into several other formats such as films, gels, particles, and scaffolds. Silks from "Bombyx mori", a kind of cultivated silkworm, are the most widely investigated silks. Silks derived from "Bombyx mori" are generally made of two parts: the silk fibroin fiber which contains a light chain of 25kDa and a heavy chain of 350kDa (or 390kDa) linked by a single disulfide bond and a glue-like protein, sericin, comprising 25 to 30
Serratiopeptidase Serratiopeptidase Serratiopeptidase (Serratia E-15 protease, also known as serralysin, serrapeptase, serratiapeptase, serratia peptidase, serratio peptidase, or serrapeptidase) is a proteolytic enzyme (protease) produced by non-pathogenic enterobacterium "Serratia" sp. E-15. This microorganism was originally isolated in the late 1960s from silkworm "Bombyx mori" L. (intestine), Serratiopeptidase is present in the silkworm intestine and allows the emerging moth to dissolve its cocoon. Serratiopeptase is produced by purification from culture of Serratia E-15 bacteria. Some alternative medicine proponents claim that serratiopeptidase is beneficial for pain and inflammation but "existing trials [have been] small and generally of poor methodological quality." Online medical journal "Bandolier"