Also known as serratiopeptidase and several other variants, serrapeptase is a micro-organism discovered in the late 1960s, with its name derived from the Greek word for silk. It comes from the intestines of the silkworm, Bombyx mori, and is an enzyme which allows the moth to dissolve its own cocoon. The enzyme digests dead tissue while leaving living tissue intact.
Serrapeptase is extracted from laboratory cultures of the Serratia E-15 bacteria and is reported to improve the efficiency of antibiotics against pathogenic bacteria, such as those found in staphylococcal infections. These bacteria have the capability to produce biofilms or protein substances which aid the bacteria in sticking to a host, or can help shield the bacteria from antibiotics designed to kill it.
Researchers reported that use of the Serratia E-15 protease was effective in eradicating infections caused by such bacteria and that it might enhance the efficacy of antibiotic treatment in relation to staphylococcal infections. If administered together with an antibiotic, serrapeptase was reported also to increase the concentration of the antibiotic at the site of the infection. Studies show that use of serrapeptase is beneficial to the reduction and loosening of mucous secretions and to help reduce inflammation.