Bombyx mori to produce proteins, including pharmacological drugs, in the place of silk proteins. "Bombyx mori" females are also one of the few organisms with homologous chromosomes held together only by the synaptonemal complex (and not crossovers) during meiosis. Kraig Biocraft Laboratories has used research from the Universities of Wyoming and Notre Dame in a collaborative effort to create a silkworm that is genetically altered to produce spider silk. In September 2010, the effort was announced as successful. Researchers at Tufts developed scaffolds made of spongy silk that feel and look similar to human tissue. They are implanted during reconstructive surgery to
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"