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Serrapeptase

Serrapeptase is an enzyme derived from silkworms. It has anti-inflammatory effects and can help prevent blood clots, but these effects are somewhat unreliable.

Our evidence-based analysis on serrapeptase features 49 unique references to scientific papers.

Kamal Patel
Research analysis led by Kamal Patel.
All content reviewed by the Examine.com Team. Published: May 4, 2014
Last Updated:

Summary of Serrapeptase

Primary Information, Benefits, Effects, and Important Facts

Serrapeptase is a proteolytic (protein destroying) enzyme from bacteria native to the digestive system of silkworms. It is the enzyme responsible for dissolving a silkworm’s cocoon.

Traditionally, serrapeptase has been used for its anti-inflammatory properties. Today, it is marketed as a joint health supplement.

Unfortunately, many studies on serrapeptase were poorly structured, with inadequate control groups. The most recent data suggests that serrapeptase is not a very effective supplement, as far as joint health and inflammation is concerned.

Though serrapeptase has been detected in plasma after supplementation, the standard oral dose for serrapeptase is low, which means very little is absorbed through the intestines. This may be one of the reasons serrapeptase is unreliable and not very effective.

Serrapeptase has been found to have the ability to liquefy mucus and reduce bacterial biofilms (reducing bacteria’s ability to stick to surfaces and each other). This means serrapeptase may be able to reduce phlegm buildup, nasal discharge, lung symptoms of cystic fibrosis and help other compounds fight bacteria. Additional research is needed to confirm these effects.

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Things To Know & Note

Primary Function:

Also Known As

Serratiopeptidase, Serratia E-15, serralysin, serratiaprotease, Serratiopeptidase, Silk worm enzymes

Goes Well With

  • Antibiotics (reduces biofilm on bacteria, and thus enhances the ability of antibiotics to act upon bacteria)

Caution Notice

Examine.com Medical Disclaimer

  • Serrapeptase, if it is to work, requires an enteric coated capsule

How to Take Serrapeptase

Recommended dosage, active amounts, other details

The standard dose for serrapeptase is 10-60mg.

Serrapeptase should be supplemented on an empty stomach, which is 30 minutes before a meal or two hours after a meal, three times a day. Most studies use 10mg of serrapeptase taken every eight hours.

More human evidence is needed to determine the optimal dose of serrapeptase. 10mg of serrapeptase is equal to approximately 20,000 enzymatic units.

Human Effect Matrix

The Human Effect Matrix looks at human studies (it excludes animal and in vitro studies) to tell you what effects serrapeptase has on your body, and how strong these effects are.
Grade Level of Evidence
Robust research conducted with repeated double-blind clinical trials
Multiple studies where at least two are double-blind and placebo controlled
Single double-blind study or multiple cohort studies
Uncontrolled or observational studies only
Level of Evidence
? The amount of high quality evidence. The more evidence, the more we can trust the results.
Outcome Magnitude of effect
? The direction and size of the supplement's impact on each outcome. Some supplements can have an increasing effect, others have a decreasing effect, and others have no effect.
Consistency of research results
? Scientific research does not always agree. HIGH or VERY HIGH means that most of the scientific research agrees.
Notes
grade-b
Inflammation
Minor High See all 4 studies
Appears to reduce swelling and inflammation following surgery or trauma, although to a lesser degree than corticosteroids. There is a lack of practical evidence for the claims behind serrapeptase (instead, studies tend to only look at post-surgery inflammation)
grade-b
Pain
Minor High See all 5 studies
When a decrease in inflammation occurs post surgery, there appears to be a concomitant reduction in pain; it tends to hover around a 1 point reduction on a VAS scale (scale of 1-10).
grade-c
Mucus Production
Notable Very High See all 4 studies
A somewhat notable decrease in mostly the viscosity of mucus (elasticity is somewhat unreliably decreased), due to the mucolytic properties of serrapeptase. This may be of use for both nasal discharge and lung sputum (cystic fibrosis)
grade-c
Breast Tenderness
Minor - See study
A decrease in breast tenderness and soreness has been noted with serrapeptase treatment in one study.
grade-c
Edema
Minor Very High See 2 studies
Related to the antiinflammatory effects, swelling and edema post surgery appear to be reduced.
grade-d
Symptoms of Carpal Tunnel
Minor - See study
A decrease in symptoms has been noted, but the study was not structurally a good one; requires replication
grade-d
Symptoms of Superficial Thrombophlebitis
Minor - See study
There appears to be a small decrease in symptoms, which is thought to be due to fibrinolytic properties of serrapeptase

Studies Excluded from Consideration

  • Confounded with paracetamol[1]

Scientific Research on Serrapeptase

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1Sources and Structure

1.1Sources

Serrapeptase is a proteolytic enzyme touted for anti-inflammatory, anti-edemic, and analgesic properties and appears to be active following oral ingestion of an enteric coated capsule.[2] Brand names for serrapeptase include Danzen, Serodase, Nemesulide, and Antiflazym.

Serrapeptase is produced from Serratia bacteria, found in the intestines of the silkworm (Bombyx mori) which sometimes leads to serrapeptase being referred to as 'silkworm enzymes'. Of the various species of serratia bacteria that can produce protease enzymes (indica, marcescens, plymuthica, and piscatorum). Serratia marcescens has a particular strain known as E15 (ATCC 13880[3]) that has up to a threefold greater yeild[4][2] and although marcescens in general is preferred for production of serrapeptase[5][6][7] the E15 strain is favored.

Serrapeptase is not the only enzyme found from these bacteria, but is the major enzyme produced (three other larger but less common enzymes are also produced).[8]

1.2Structure

The serrapeptase enzyme has a molecular weight of 45,000-60,000Da (50.6kDa reported elsewhere[9]) and is comprised of 470 amino acids in length; it is classified as a metalloprotease due to containing a zinc molecule which helps catalyze its enzymatic activity.[8][10] Although it shows maximal activity at 40°C and a pH of 9.0, it is fully inactivated at 55°C for 15min[10][2] and possesses an isoelectric point of 5.3.[8]

It's substrate specificity appears to be somewhat similar to that of thermolysin (produced from bacillus thermoproteolyticus),[10] and the amino acid sequence is free of sulfur containing amino acids (cysteine and methionine).[8]

Appears to be a rather large metalloprotease enzyme, which can be inactivated (rendered useless) by excess heat

2Pharmacology

2.1Absorption

Due to the supplement in question being an enzyme and destroyed in the acidic environment of the stomach,[8] enteric coated capsules (resistant to acidity, and thus degrade in the intestines rather than the stomach[11]) are used. Aquasomes (a carrier comprised of a nanocrystalline core coated with polyhydroxy oligomers[12]) follow a similar idea, where it is stable for 2-6 hours in acidic medium (pH 1.2) and has a linear release rate in alkaline medium (pH 7.4).[13]

Serrapeptase is destroyed in the acidic environment of the stomach, and as such would require enteric encapsulation in order to retain the bioactivity

Despite being a large protein structure, serrapeptase has been found to be absorbed in the rat intestine following oral administration,[14] although the large structure and possible degradation in the intestines has been cited to possible reduce the bioavailability of serrapeptase (enzymes are readily degraded by drastic changes in pH and large protein structures may not be absorbed well[15]).

Serrapeptase alone appears to have low permeability in a Caco-2 model of intestinal permeability (–7.72+/- 0.51cm/s[16]) which appears to slightly improved with liposomal delivery systems (phosphatidylcholine up to -7.47+/-0.36cm/s and 1,2-dimyristoyl-sn-glycero-3-phosphoethanolamine up to -6.5+/-0.35cm/s).[16] It was noted that this may underestimate the absorption of serrapeptase a bit, as Caco-2 cells have tighter gap junctions than do in vivo conditions (and thus less paracellular transport).[16]

The enhanced absorption of serrapeptase with liposomes is thought to due to liposomes increasing paracellular (between cells) transport of molecules[17][18] and serrapeptase being too large for transport-mediated absorption (and thus likely mediated by paracellular transport).

Serrapeptase, surprisingly, is absorbed through the intestinal wall similar to bromelain and appears to retain its enzymatic activity. It appears to be absorbed paracellularly (between cells), but does not appear to be well absorbed although it is enhanced by liposomes

Serrapeptase has been thought to be used topically, although isopropyl myristate (IPM) or dimethyl sulfoxide (DMSO) are required to enhance skin absorption (due to serrapeptase being a large enzyme structure) and were required at higher than acceptable concentrations according to the authors.[19] In a rat anti-edema test, a topical gel (Monegyl 0100 at 10%, PEG 400 at 40%, Propylene glycol at 10%, 1% serrapeptase, and PEG 4000 added until mixture congeals) was comparable in efficacy to a diclofenac gel suggesting some bioactivity.[19]

Other delivery methods that have been reported are a glyceryl monooleate based system.[20]

There is limited evidence that serrapeptase can be bioactive topically, which needs to be re-evaluated and mechanisms investigated more (as it is quite illogical for a large protein structure to be absorbed via the skin)

2.2Serum

It has been detected in serum following an oral dose of 100mg/kg (rats) to 0.87+/-0.41ng/mL, and in lymph it had higher concentrations of 43+/-42ng/mL at a Tmax of 15-30 minutes.[14] A minimum dose of 30mg/kg was required to find any detectable concentration in plasma, yet only 1mg/kg for a level in lymph tissue.[14]

In rats it appears to travel through the blood bound to plasma protease inhibitor alpha-1 macroglobulin (α1M) in a 1:1 ratio; this has been noted to reduce the enzymatic activity to about 20% of its inhernet value, but a value still appears to be present.[21]

2.3Distrubution

Serrapeptase has been found to be distributed to sites of inflammation in the rat (careegnaan induced) to a concentration higher than serum.[14]

3Neurology

3.1Pain

Pain has been noted to be reduced on days 1-5 after jaw surgery with 15mg serrapeptase relative to placebo (study confounded with 1000mg paracetamol in both groups) but no significant difference on day 7, with a 3 point reduction on day 1 (VAS scale; a rating from 0-10) and a 1 point difference afterwards.[1]

A study in breast pain (engorgement and swelling) noted that 30mg of serrapeptase for 3 days was able to increase the amount of response (persons who reported pain reduction) from 60% to 85.7% and increase reported 'marked improvements' in pain from 2.9% in placebo to 22.9%.[22]

4Inflammation and Immunology

4.1Mechanisms

It is claimed that the enzymatic activity of serrapeptase (appears to be somewhat preserved following oral ingestion) is able to hydrolyze bradykinin, histamine and serotonin which are responsible for edemic processes.[23][24]

4.2Small Joint Inflammation

10mg of serrapeptase thrice a day the day prior to and of surgery (maxillary sinus antrotomy) as well as for 5 subsequent days (7 days in total), relative to placebo, was able to significantly reduce jaw swelling at all measured time points.[25]

In patients undergoing removal of third molars given paracetamol (1000mg) paired with serrapeptase (15mg daily, 5mg taken every 8 hours for 7 days) or placebo, there was a significantly reduction in cheek swelling on all measured days except immediately after surgery while pain followed the opposite trend (significantly more effective than placebo days 1-5 after surgery, but not day 7); interincisal difference was not affected.[1] Other studies on third molar surgeries noted that either serrapeptase is ineffective in reducing inflammation[26] or the standard 30mg dose is effective, but to a lesser degree than 3mg dexamethasone (1mg thrice daily).[27]

The research looking at jaw inflammation appears to support the usage of serrapeptase, but aside from the studies being limited it appears to be less effective than the reference drug (dexamethasone)

One study in carpal tunnel syndrome given an initial course of nimesulide and then followed up with 10mg serrapeptase twice daily (20mg daily) for 6 weeks noted a 65% response rate for 'significant improvement' but did not have a placebo group for comparison.[28]

The evidence to support a role in carpal tunnel syndrome is, methodologically speaking, quite weak

4.3Other Interventions

In rats, the anti-inflammatory effects of serrapeptase at 10-20mg/kg was compaed against 0.5mg/kg diclofenac (for both an acute inflammation study over 8 hours and a chronic inflammation study over 9 days) noted that all groups were comparable in reducing paw edema acutely (43.18-54.55% suppression of paw edema) but there appeared to be dose-dependence for chronic inflammation where 10mg/kg serrapeptase underperformed diclofenac (40% inhibition of paw edema relative to 72%) while 20mg/kg was comparable (68% relative to 72%).[24]

Anti-inflammatory effects appear to exist in rats following oral ingestion

A meta-analysis[2] of 14 trials noted that the six positive trials included (five can be found online[29][22][28][30][25]) were fairly low quality, with three trials not disclosed the given dose and one not compared to any control or placebo group; the final two studies that were positive were in treating jaw swelling after maxillary sinus antrotomy surgery[25] and for reducing breast engorgement ('marked improvement' was 22.9% with serrapeptase, 2.9% with placebo);[22] both studies used 30mg daily in three doses of 10mg for 7-14 days.

The studies that support the efficacy of serrapeptase appear to be low in quality

4.4Biofilms and Mucus

In staphylococci bacteria (epidermidis and aureus populating human skin and mucus membranes) are bacteria that can produce protein-dependent biofilms[31][32] and protease enzymes are a class of molecules which are sometimes used to disperase these biofilms.[33] At 50U/mL (2.5mcg/mL), serrapeptase was able to inhibit biofilm production of all tested strains (aureus strains ATCC 6538P, 25923, 35984, and 12598 as well as epidermis strains XX-17 and O-47).[34][35] Efficacy has also been noted against 5 strains of Pseudomonas aeruginosa[9] and Listeria monocytogenes.[36]

In a comparative analysis, serrapeptase was more potent than other tested proteases (Clostridiopeptidase A, fibrinolysin, and streptokinase).[9]

For bacteria that create protein-dependent biofilms, it appears that serrapeptase may have an inhibitory effect on biofilm production

Biofilms are used by bacteria to, aside from adherence to cells, to prevent infiltration of the bacteria cell from antibacterial agents[37][38] and in vitro serrapeptase (100U/mL; 5mcg/mL) has been found to augment the anti-bacterial properties of ofloxacin by approximately halving the minimum inhibitory concentration.[9]

In vitro, serrapeptase has been found to augment antibacterials which is thought to be from reducing biofilm production (which then enhances the ability of the antibacterial agent to target the bacteria since it is removing the bacterial defenses). These have not yet been noted in a living model

Serrapeptase is known as a mucus liquifying agent[39] and 30mg of serrapeptase daily for 4 weeks in persons with chronic airway diseases has been noted to significantly decrease sputum weight and neutrophil count as well as its viscosity and elasticity;[40] a significant decrease in the frequency of coughing and expectoration was also noted.[40]

Elsewhere, serrapeptase has been noted to reduce dynamic viscosity of nasal secretion with affecting the elastic modulus[41] and this effect (a reduction in viscosity but not elasticity) has been noted elsewhere following oral ingestion of 30mg serrapeptase daily for 4 weeks.[42] Other studies, however, either note a decrease in both viscosity and elasticity (lung sputum)[40] or a decrease in viscoelasticity.[43] While the decrease in viscosity appears to be reliable, the elasticity is not as much.

Appears to alter mucus secretions of the body. Although there is not an ample amount of evidence for this, it may be of use to persons with chronically stuffed noses (sinusitis) and for lung symptoms of cystic fibrosis (currently untested)

The biofilm reducing properties of serrapeptase have also been noted to be of use in rats given a surgery with risk for infection afterwards (by biofilm producing bacteria), where the occurrence rates of bacterial growth on the surgical site of 63.2% (control) was reduced with antibiotic treatment (37.5%) and synergistically reduced with the addition of serrapeptase to antibiotics (5.6%).[44]

5Nutrient-Nutrient Interactions

5.1Antibiotics

Serrapeptase appears to be synergistic with antibiotic drugs and molecules. Serrapeptase has the ability to reduce the biofilms produced by select bacteria and these biofilms can impair the ability of antibiotics to destroy a bacteria.[37][38]

In vitro, serrapeptase (100U/mL; 5mcg/mL) has been found to augment the anti-bacterial properties of ofloxacin by approximately halving the minimum inhibitory concentration[9] and in a rat model of surgery where the occurrence of bacterial infection in control (63.2%) was reduced to 37.5% with antibiotics but down to 5.6% with the combination treatment of antibiotics and serrapeptase.[44]

Elsewhere in rabbits, the plasma concentrations of Cefotiam appear to be increased following coingestion of serrapeptase, while only increasing tissue concentrations in the rabbit model of pneumonitis (no effect in pleuritis)[45] and has been noted to increae gingival concentrations of four antibiotic drugs (Ciclacillin, ampicillin, cephalexin, and minocycline) in rats given 20mg/kg serrapeptase.[46]

Appears to augment antibiotic efficacy by reducing the inhibitory effects of bacterial biofilms

5.2Aspirin

One study assessing the interactions of injections of proteolytic enzymes (Serrapeptase, chymotrypsin, or trypsin) and aspirin noted that all enzymes were synergistic with aspirin in acute and subacute inflammatory tests in rats;[47] this study also noted that 90-270µg/kg serrapeptase was equivalent to 200mg/kg (oral ingestion) and was equivalent to trypsin (288-576µg/kg) and chymotrypsin (18-36mg/kg) in potency.[47]

6Safety and Toxicity

6.1General

A systemic review on serrapeptase[2] has noted that there are limited adverse drug reactions reported, but they tend to be related to skin conditions (such as erythema or dermatosis[48]) and both muscle and joint pain; there appear to be some reported coagulation problems.[2]

Commonly said to be safe (although there really isn't any robust toxicological data on this claim) and has been linked to sporadic side-effects related to joints and the skin. Occurrence rates are not known, but they seem rare

References

  1. ^ a b c Al-Khateeb TH, Nusair Y. Effect of the proteolytic enzyme serrapeptase on swelling, pain and trismus after surgical extraction of mandibular third molars. Int J Oral Maxillofac Surg. (2008)
  2. ^ a b c d e f Bhagat S, Agarwal M, Roy V. Serratiopeptidase: a systematic review of the existing evidence. Int J Surg. (2013)
  3. ^ Badhe RV, et al. Media optimization studies for Serratiopeptidase production from Serratia marcescens ATCC 13880. Hindustan Antibiot Bull. (2009)
  4. ^ Purification and characterization of four proteases from a clinical isolate of Serratia marcescens kums 3958.
  5. ^ Pansuriya R, Singhal R. Effects of dissolved oxygen and agitation on production of serratiopeptidase by Serratia marcescens NRRL B-23112 in stirred tank bioreactor and its kinetic modeling. J Microbiol Biotechnol. (2011)
  6. ^ CASTANEDA-AGULLO M. Studies on the biosynthesis of extracellular proteases by bacteria. I. Serratia marcescens, synthetic and gelatin media. J Gen Physiol. (1956)
  7. ^ Bromke BJ, Hammel JM. Regulation of extracellular protease formation by Serratia marcescens. Can J Microbiol. (1979)
  8. ^ a b c d e Matsumoto K, et al. Purification and characterization of four proteases from a clinical isolate of Serratia marcescens kums 3958. J Bacteriol. (1984)
  9. ^ a b c d e Selan L, et al. Proteolytic enzymes: a new treatment strategy for prosthetic infections. Antimicrob Agents Chemother. (1993)
  10. ^ a b c Cloning and sequencing of Serratia protease gene.
  11. ^ Easily absorbable enzyme preparation.
  12. ^ Umashankar MS, Sachdeva RK, Gulati M. Aquasomes: a promising carrier for peptides and protein delivery. Nanomedicine. (2010)
  13. ^ Rawat M, et al. Development and in vitro evaluation of alginate gel-encapsulated, chitosan-coated ceramic nanocores for oral delivery of enzyme. Drug Dev Ind Pharm. (2008)
  14. ^ a b c d Moriya N, et al. Intestinal absorption of serrapeptase (TSP) in rats. Biotechnol Appl Biochem. (1994)
  15. ^ Woodley JF. Enzymatic barriers for GI peptide and protein delivery. Crit Rev Ther Drug Carrier Syst. (1994)
  16. ^ a b c KV S, Devi GS, Mathew ST. Liposomal formulations of serratiopeptidase: in vitro studies using PAMPA and Caco-2 models. Mol Pharm. (2008)
  17. ^ Camenisch G, Folkers G, van de Waterbeemd H. Shapes of membrane permeability-lipophilicity curves: extension of theoretical models with an aqueous pore pathway. Eur J Pharm Sci. (1998)
  18. ^ Obata K, et al. Prediction of oral drug absorption in humans by theoretical passive absorption model. Int J Pharm. (2005)
  19. ^ a b Nirale NM, Menon MD. Topical formulations of serratiopeptidase: development and pharmacodynamic evaluation. Indian J Pharm Sci. (2010)
  20. ^ Shah MH, Paradkar A. Cubic liquid crystalline glyceryl monooleate matrices for oral delivery of enzyme. Int J Pharm. (2005)
  21. ^ Kakinuma A, et al. Repression of fibrinolysis in scalded rats by administration of Serratia protease. Biochem Pharmacol. (1982)
  22. ^ a b c Kee WH, et al. The treatment of breast engorgement with Serrapeptase (Danzen): a randomised double-blind controlled trial. Singapore Med J. (1989)
  23. ^ Malshe PC. A preliminary trial of serratiopeptidase in patients with carpal tunnel Syndrome. J Assoc Physicians India. (2000)
  24. ^ a b Jadav SP, et al. Comparison of anti-inflammatory activity of serratiopeptidase and diclofenac in albino rats. J Pharmacol Pharmacother. (2010)
  25. ^ a b c Tachibana M, et al. A multi-centre, double-blind study of serrapeptase versus placebo in post-antrotomy buccal swelling. Pharmatherapeutica. (1984)
  26. ^ Chopra D, et al. A randomized, double-blind, placebo-controlled study comparing the efficacy and safety of paracetamol, serratiopeptidase, ibuprofen and betamethasone using the dental impaction pain model. Int J Oral Maxillofac Surg. (2009)
  27. ^ Murugesan K, Sreekumar K, Sabapathy B. Comparison of the roles of serratiopeptidase and dexamethasone in the control of inflammation and trismus following impacted third molar surgery. Indian J Dent Res. (2012)
  28. ^ a b Panagariya A, Sharma AK. A preliminary trial of serratiopeptidase in patients with carpal tunnel syndrome. J Assoc Physicians India. (1999)
  29. ^ Esch PM, Gerngross H, Fabian A. Reduction of postoperative swelling. Objective measurement of swelling of the upper ankle joint in treatment with serrapeptase-- a prospective study. Fortschr Med. (1989)
  30. ^ Bracale G, Selvetella L. Clinical study of the efficacy of and tolerance to seaprose S in inflammatory venous disease. Controlled study versus serratio-peptidase. Minerva Cardioangiol. (1996)
  31. ^ Relevant Role of Fibronectin-Binding Proteins in Staphylococcus aureus Biofilm-Associated Foreign-Body Infections.
  32. ^ Christner M, et al. The giant extracellular matrix-binding protein of Staphylococcus epidermidis mediates biofilm accumulation and attachment to fibronectin. Mol Microbiol. (2010)
  33. ^ Kaplan JB. Biofilm dispersal: mechanisms, clinical implications, and potential therapeutic uses. J Dent Res. (2010)
  34. ^ Artini M, et al. Comparison of the action of different proteases on virulence properties related to the staphylococcal surface. J Appl Microbiol. (2013)
  35. ^ Artini M, et al. A new anti-infective strategy to reduce adhesion-mediated virulence in Staphylococcus aureus affecting surface proteins. Int J Immunopathol Pharmacol. (2011)
  36. ^ Longhi C, et al. Protease treatment affects both invasion ability and biofilm formation in Listeria monocytogenes. Microb Pathog. (2008)
  37. ^ a b Influence of interfaces on microbial activity.
  38. ^ a b Costerton JW, et al. Bacterial biofilms in nature and disease. Annu Rev Microbiol. (1987)
  39. ^ Lee HS, et al. A technique for quantitative cytology of nasal secretions. Eur Arch Otorhinolaryngol. (1991)
  40. ^ a b c Nakamura S, et al. Effect of the proteolytic enzyme serrapeptase in patients with chronic airway disease. Respirology. (2003)
  41. ^ Majima Y, et al. Effects of orally administered drugs on dynamic viscoelasticity of human nasal mucus. Am Rev Respir Dis. (1990)
  42. ^ Majima Y, et al. The effect of an orally administered proteolytic enzyme on the elasticity and viscosity of nasal mucus. Arch Otorhinolaryngol. (1988)
  43. ^ Shimura S, et al. Effect of expectorants on relaxation behavior of sputum viscoelasticity in vivo. Biorheology. (1983)
  44. ^ a b Mecikoglu M, et al. The effect of proteolytic enzyme serratiopeptidase in the treatment of experimental implant-related infection. J Bone Joint Surg Am. (2006)
  45. ^ Ishihara Y, Kitamura S, Takaku F. Experimental studies on distribution of cefotiam, a new beta-lactam antibiotic, in the lung and trachea of rabbits. II. Combined effects with serratiopeptidase. Jpn J Antibiot. (1983)
  46. ^ Aratani H, Tateishi H, Negita S. Studies on the distributions of antibiotics in the oral tissues: Experimental staphylococcal infection in rats, and effect of serratiopeptidase on the distributions of antibiotics (author's transl). Jpn J Antibiot. (1980)
  47. ^ a b Viswanatha Swamy AH, Patil PA. Effect of some clinically used proteolytic enzymes on inflammation in rats. Indian J Pharm Sci. (2008)
  48. ^ Shimizu H, et al. A case of serratiopeptidase-induced subepidermal bullous dermatosis. Br J Dermatol. (1999)
  49. Mazzone A, et al. Evaluation of Serratia peptidase in acute or chronic inflammation of otorhinolaryngology pathology: a multicentre, double-blind, randomized trial versus placebo. J Int Med Res. (1990)

This page is regularly updated, to include the most recently available clinical trial evidence.

Each member of our research team is required to have no conflicts of interest, including with supplement manufacturers, food companies, and industry funders. The team includes nutrition researchers, registered dietitians, physicians, and pharmacists. We have a strict editorial process.

This page features 49 references. All factual claims are followed by specifically-applicable references. Click here to see the full set of references for this page.

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