Serrapeptase Article 1

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Serratiopeptidase (Serratia E-15 protease, also known as serralysin, serratiapeptase, serratia peptidase, serratio peptidase, or serrapeptidase) is a proteolytic enzyme (protease) produced by enterobacterium Serratia sp. E-15.[1] This microorganism was originally isolated in the late 1960s from silkworm Bombyx mori L. (intestine),[2] 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.

Claims of anti-inflammatory benefits

Some alternative medicine proponents claim that serratiopeptidase is beneficial for pain and inflammation[3] but there is no compelling evidence.[4] Online medical journal Bandolier (specializing in Evidence-based thinking about healthcare)[5] published an article (in about 2001) in response to a reader's enquiry about serratiopeptidase.[6] After searching PubMed and the Cochrane Library "to see if there are any randomised, controlled trials", the article stated that the "evidence on serratiopeptidase being effective for anything is not based on a firm foundation of clinical trials."[4]
The search found 34 publications in the medical databases covered, that addressed the efficacy of serratiopeptidase, of which several were found to be animal experiments, personal letters, uncontrolled trials or those with inadequate or nonexistent randomisation. The article warned against ignoring safety issues with use of biological agents.[4] No studies were found to have been conducted on the efficacy of serratiopeptidase as treatment for back pain, heart attack, stroke, or asthma. Of the 10 medical conditions with randomized-evidence studies on file in connection with serratiopeptidase, trial quality was described as "generally poor".[7][4]

See also
Proteases (medical and related uses)

References

^ Nakahama K, Yoshimura K, Marumoto R, Kikuchi M, Lee IS, Hase T, Matsubara H (July 1986). "Cloning and sequencing of Serratia protease gene". Nucleic Acids Res. 14 (14): 5843 55. PMID 3016665.
^ The preparation and some uses of the protease are described in US patent 3792160, Isono M, Kazutaka M, Kodama R, Tomoda K, Miyata K, "Method of treating inflammation and composition therefor", granted 1974-02-12 , assigned to Takeda Chemical Industries Ltd.. The enzyme was also described by Miyata K, Maejima K, Tomoda K, Isono M (1970). "Serratia protease. Part I. Purification and general properties of the enzyme". Agricultural and Biological Chemistry 34 (2): 310-318. http://www.journalarchive.jst.go.jp/jnlpdf.php?cdjournal=bbb1961&cdvol=34&noissue=2&startpage=310&lang=en&from=jnlabstract. and the strain of bacteria producing serratiopeptidase has been deposited with the American Type Culture Collection as strain ATCC 21074. (For online information about ATCC 21074, enter 21074 on the ATCC/LGC search page)
^ C.K. Kokate. Pharmacognosy. p. 12.11.
^ a b c d "Serratiopeptidase: Finding the Evidence" (HTML). Bandolier online edition. http://www.medicine.ox.ac.uk/bandolier/booth/alternat/serrapep.html. Retrieved 2008-03-20.
^ Bandolier online home-page
^ The Bandolier article is undated and unsigned but the text indicates that it was written in response to a letter sent by a reader of a newspaper article that was published in 2001. No references later than 2001 are cited.
^ According to Bandolier:
"Studies were small, outcomes were poorly defined, and in some, different medical conditions were mixed. Five studies were described as double blind: one was completely uninterpretable, three methodologically weak studies were positive, and one trial of apparent high quality was negative. This latter study compared serratiopeptidase, serraprose S or placebo in the treatment of chronic respiratory disease, with about 120 patients per group, and found no significant difference between groups for any outcome."
- Bandolier, "Serratiopeptidase - Finding the Evidence"
Retrieved from "http://en.wikipedia.org/wiki/Serratiopeptidase"
Categories: Biologically based therapies