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Serratiopeptidase (Serratia E-15 protease, also known as serralysin, serrapeptase, serratiapeptase, serratia peptidase, serratio peptidase, or serrapeptidase) is a proteolytic enzyme (protease) produced by enterobacteriumSerratia sp. E-15, now known as Serratia marcescens ATCC 21074.[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. It is a member of the Peptidase M10B (Matrixin) family.
Serralysin
Crystal structure of serralysin with co-ordinated zinc (grey) and calcium (white). Rendered from PDB 1SAT.
Some alternative medicine proponents claim that serratiopeptidase is beneficial for pain and inflammation[3] but "existing trials [have been] small and generally of poor methodological quality."[4] Online medical journalBandolier (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, the quality or construction of the trial studies was described as "generally poor".[4][7]
^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 Research. 14 (14): 5843–55. doi:10.1093/nar/14.14.5843. PMC311595. 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", issued 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. 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)
^ abcd"Serratiopeptidase: Finding the Evidence". Bandolier online edition. Retrieved 2008-03-20.
^"Bandolier - Evidence based thinking about health care".
^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.
"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"
External linksedit
The MEROPS online database for peptidases and their inhibitors: M10.051
serratiopeptidase, this, article, multiple, issues, please, help, improve, discuss, these, issues, talk, page, learn, when, remove, these, template, messages, neutrality, this, article, disputed, relevant, discussion, found, talk, page, please, remove, this, m. This article has multiple issues Please help improve it or discuss these issues on the talk page Learn how and when to remove these template messages The neutrality of this article is disputed Relevant discussion may be found on the talk page Please do not remove this message until conditions to do so are met April 2013 Learn how and when to remove this message This article needs more reliable medical references for verification or relies too heavily on primary sources Please review the contents of the article and add the appropriate references if you can Unsourced or poorly sourced material may be challenged and removed Find sources Serratiopeptidase news newspapers books scholar JSTOR July 2012 Learn how and when to remove this message Serratiopeptidase Serratia E 15 protease also known as serralysin serrapeptase serratiapeptase serratia peptidase serratio peptidase or serrapeptidase is a proteolytic enzyme protease produced by enterobacterium Serratia sp E 15 now known as Serratia marcescens ATCC 21074 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 It is a member of the Peptidase M10B Matrixin family SerralysinCrystal structure of serralysin with co ordinated zinc grey and calcium white Rendered from PDB 1SAT IdentifiersEC no 3 4 24 40CAS no 70851 98 8DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumSearchPMCarticlesPubMedarticlesNCBIproteins SerratiopeptidaseIdentifiersOrganismSerratia sp E 15SymbolSpro 0210Entrez5605823PDB1SRPUniProtP07268Other dataEC number3 4 24 40Search forStructuresSwiss modelDomainsInterPro Contents 1 Health claims 2 See also 3 References 4 External linksHealth claims editSome alternative medicine proponents claim that serratiopeptidase is beneficial for pain and inflammation 3 but existing trials have been small and generally of poor methodological quality 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 the quality or construction of the trial studies was described as generally poor 4 7 See also editProteases medical and related uses References edit 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 Research 14 14 5843 55 doi 10 1093 nar 14 14 5843 PMC 311595 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 issued 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 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 Kokate CK Purohit AP Gokhale SB 2008 Pharmacognosy 14th ed Mumbai Nirali Prakashan p 12 11 ISBN 978 81 85790 09 1 a b c d Serratiopeptidase Finding the Evidence Bandolier online edition Retrieved 2008 03 20 Bandolier Evidence based thinking about health care 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 External links editThe MEROPS online database for peptidases and their inhibitors M10 051 Portal nbsp Biology Retrieved from https en wikipedia org w index php title Serratiopeptidase amp oldid 1172360776, wikipedia, wiki, book, books, library,
