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Do Enzymes For Yeast Infection and Candida Really Work?

Medically Reviewed by Dr. Atmika Paudel & Dr. Vibhuti Rana

Enzymes for yeast eat the cell wall of Candida and other yeasts because the cell wall is composed of fiber and glycoproteins. Many times the patient will not experience any die-off reaction at all, especially when using an enzyme that contains protease, which is a huge bonus.

Lets review the basic cell and biofilm structure of yeasts.

Yeast Cell Structure Review

Candida yeast has a cell wall composed of mannoprotein-1, glucan, chitin-glucan, mannoprotein-2 and plasma membrane.

A mannoprotein is a complex carbohydrate-modified protein used by yeasts to anchor the proteins to the cell wall glucans.

Glucans are a polysaccharide fiber, that are found in the cell walls of bacteria, fungi, algae, lichens and plants such as oats and barley.

Chitins are long-chain polymer of N-acetylglucosamine, which is a derivative of glucose. It is a primary component of fungal cell walls and the exoskeletons of arthropods. It is very similar to the polysaccharide cellulose - the basic fiber component of plant cell walls.

The plasma membrane is a fatty lipid and protein layer and the nucleus of the yeast cell is also made of protein.

The fatty acids oleic, linolic, palitic, and palmitolic are found throughout its structure.

Knowing that the cell wall of Candida yeast is made up of proteins with carbohydrate rich fibers including a protein and lipid nucleus, a properly designed enzyme formula should contain the necessary enzymes to digest all of these parts.

Dr. Atmika Paudel says...

Basically, cell wall are made up of carbohydrates and proteins, and play a vital role in recognition of immune cells inside the host, and adhesion to the host cells. The information about the components of Candida cell structure are correct.

Dr. Vibhuti Rana says…

The Candida cell wall is a strong structural feature of the yeast, having high proportions of fibrillar polysaccharides and proteins. These can be adherent proteins (having glyco-phosphatidylinositol linkage), secretory proteins (having N-terminal signal peptide), and another set of proteins for which surface association is unknown. (1)

Moreover, Mishra and Prasad, in a book published in 1991, discussed that the first step or initiation of fungal infection is by lipid mediated adherence to host cells. Among these, neutral lipids and phospholipids are major constituents. Some of them are triacylglycerol, diacylglycerol, fatty acids, sterols, phosphatidylcholine, phosphatidylethanolamine , phosphatidylserine, and phosphatidylinositol (PI). In addition, some fatty acids that are unique to Candida species are linoleic and linolenic acids, which have varied levels during the different morphological transitions of yeast. (2)

1. W. LaJean Chaffin, Microbiology and Molecular Biology Reviews Sep 2008,72 (3) 495-544; DOI: 10.1128/MMBR.00032-07.
2. Mishra P., Prasad R. (1991) Lipids of Candida albicans. In: Prasad R. (eds) Candida Albicans. Springer, Berlin, Heidelberg.

Yeast Biofilm Structure Review

Biofilms are used by pathogenic yeasts, bacteria and viruses as a way to hide from the hosts immune system. At the same time the pathogen will release spores or cells in an attempt to spread throughout the body. Upon release of the spores the immune system mounts a defense, which causes inflammation and can make you feel sick.

Yeast biofilms generally contain parts of the cell wall structure itself.

It will be composed of cellulose, which is basically a chain of polysaccharide fibers.

The biofilm will also contain polynucleotides that are made from bonded sugars and are primarily its dna and rna material.

Also present are polypeptide proteins and carbohydrate glucan polysaccharides.

The biofilm also contains fibrinogen and fibronectin or scar tissue, which are the same materials that the body uses to clot the blood and repair wound sites.

All of these materials are bound together by ligands with stickiness properties much like lectins in wheat.

The biofilm will form in the section of the picture above marked F. The biofilm is the first thing you need to get through in order to have any effect on the yeast cell itself.

So, the biofilm is made from proteins, with carbohydrate rich fibers much like the cell wall. In addition, microorganisms such as bacteria and yeast use fibrinogen and fibronectin to adhere and make biofilms with the help of fibronectin binding proteins present in these microorganisms. More on the cell structure and biofilms here.

Dr. Atmika Paudel says...

A paper published in 2017 in Journal of Fungi gives a detail about the composition of the biofilms of Candida. Biofilms are composed of carbohydrates and proteins in addition to lipids and nucleic acids. By forming biofilms, Candida hides itself into the protection of the biofilm and becomes resistant to many antifungal agents.

Dr. Vibhuti Rana says…

Biofilm is an extracellular matrix, made up of exopolymeric materials, and is a characteristic feature of Candida pathogenesis, the third/fourth most common infection in US hospitals. Biofilm formation is affected by alterations in temperature, pH, growth medium, etc. Proteins constitute more than 55% of the dry mass of biofilm, followed by carbohydrates (25%), lipids (15%), and nucleic acids (5%). (1)

Biofilms enable the pathogens to escape from the host immune response and the drug effects. Biofilms pose a serious problem as they can also grow on medical devices, such as prostheses, cardioverter defibrillators, urinary and vascular catheters, and cardiac devices, further obstructing the elimination of Candida infections. (2)

1. Pierce CG, Vila T, Romo JA, et al. The Candida albicans Biofilm Matrix: Composition, Structure and Function. J Fungi (Basel). 2017;3(1):14. doi:10.3390/jof3010014.
2. Cavalheiro M, Teixeira MC. Candida Biofilms: Threats, Challenges, and Promising Strategies. Front Med (Lausanne).
2018
;5:28. Published 2018 Feb 13. doi:10.3389/fmed.2018.00028.

Enzymes Needed for The Best Results

For the mannoproteins in the cell, polypeptide proteins in the biofilm, and the nucleus of the yeast cell you need a protease enzyme.

The glucans and cellulose-chitin found in both the cell wall and biofilm you need cellulase and hemicellulase. Beta-glucanase is also very helpful but a quality cellulase will have beta-glucanase side activity so you're covered in that respect.

The polysaccharides found in both the cell and biofilm can be removed with amylase, invertase and glucoamylase.

The fibrinogen, fibronection and the ligands in the biofilm can be removed with serrapeptase(serratiopeptidase).

For the fatty lipids a lipase enzyme would work.

In our opinion, getting through the biofilm is the most important aspect when treating yourself for candida yeast infections. If you don't get through the biofilm, you are not going to have any long term success getting the yeast under control.

What enzyme for yeast brands are the best to use? See our review here

Do Enzymes for Yeast Really Work on the Cell Wall?

Way back in 1968 Roberte Domanski and Ruth Miller from the Dept. of Microbiology at the Women's Medical College of Pennsylvania, used a chitanase complex and beta-glucanase on the cell walls of Candida albicans. Within 5 minutes of exposure to the enzymes in the presence of water, the cell walls burst. Note the intact cells in picture 1 and the disrupted cell in picture 2.

In 1971 Canadian scientist Joseph Brown analyzed the helicase enzyme from the snail Helix pomatia, effects on the cells of Torulopsis glabrata, Candida albicans, and Saccharomyces cerevisiae. He noted that the effects of the enzyme on Candida glabrata wore off in a couple of hours as the fungi adapted to the effects of the enzyme. It took much longer for the other two yeast cell walls to adapt to the enzyme.(1)

In 1976 the effects of enzymes on the cell surface of Candida Albicans was examined at the Department of Biochemistry, The University, in Leeds. Beta-glucanase worked well but major changes took place with the addition of chitanase and protease, which resulted in the greatest disruption of the cell wall.(2)

In 1980, E. F. Gale and associates ran enzyme studies on the cell structure of Candida albicans to see if they would help reduce the organisms ability to resist Amphotericin B. They found that beta-glucanase had the greatest effects on the cell wall. They also found that the effects were further enhanced when using chitinase, trypsin - which is a protease, or lipase.(3)

A 2003 study in Belgium evaluated the effects of the enzymes protease and amyloglucosidase on the yeast Saccharomyces cerevisiae. It was found that the protease caused a progressive increase of surface roughness. Large depressions surrounded by protruding edges were formed and attributed to the erosion of the mannoprotein outerlayer. The amyloglucosidase had no effect, which is what they expected based on the cell structure of Saccharomyces cerevisiae. The study also noted that Saccharomyces cerevisiae is susceptible to protease.(4)

In Sept of 2017, a study was performed in South Korea at the College of Agricultural and Life Science on the fungi Fusarium oxysporum and Rhizoctonia solani. Chitanase and Beta-glucanase enzymes were used to see if they had any effect on the cell wall structure. The enzymes were found to inhibit hyphael growth of these two species.(5)

Because Candida yeast is also a fungi with similar cell structure, there is no reason to not believe that these enzymes would not work on hyphael producing strains of Candida. 

What have we learned from these studies?

  • In every study the enzymes did have an effect on the cell wall.
  • Using multiple enzymes had the greatest effects.

  • Beta-glucanase seems to be the best enzyme but alone is not the answer either. It should be noted, according to our lab testing, a quality cellulase will have beta-glucanase side activity.

  • A quality cellulase will also have Chitinase side activitiy.

  • Protease does indeed work on the mannoproteins found in the cell walls of yeasts. Its effects can be further enhanced by the addition of cellulases and lipase.

The obvious conclusion, based on the uses of these enzymes singularly and when combined, is to use an enzyme formula that has all the necessary enzymes required to digest every component of the cell wall. The studies suggest that complete formulas are going to have the greatest effects.

Dr. Vibhuti Rana says..

Biofilms are a hard to remove source of infection caused by yeast pathogens. Anti‐biofilm enzymes can target the cells embedded in the matrix and promote cell lysis. Nonetheless, these enzymes mainly focus on the extracellular polymeric substances (EPS) and break down the cell‐to‐cell connectively, along with degrading the matrix macromolecules. (1)

In the past, disruption of biofilms has been tried by use of acids/bases, or disinfectants, to a negligible benefit. Therefore, enzymatic removal of biofilms remains the main method of these contaminating extracellular polymeric substances (EPS) containing biofilms. Research shows that a selected cocktail of enzymes, isolated from different strains, work best at targeting biofilm matrix. (2) The terpenic derivatives have also shown some promising results in biofilm tackling.

1. Nahar, S., Mizan, M.F.R., Ha, A.J.‐w. and Ha, S.‐D. (2018), Advances and Future Prospects of Enzyme‐Based Biofilm Prevention Approaches in the Food Industry. Comprehensive Reviews in Food Science and Food Safety, 17: 1484-1502. doi:10.1111/1541-4337.12382
2. Gauthier Boels (2011) Enzymatic removal of biofilms: A report, Virulence, 2:5, 490-489, DOI: 10.4161/viru.2.5.17317

Do Enzymes for Yeast Really Work on the Biofilm?

Yes they do and they work extremely well. They also work for bacterial biofilms as we're going to prove to you. This is very important because half of the stool tests we see show no yeast but over growths of pathogenic bacteria.

A published study in 2006 that was done at the Institute of Biomedical and Life Sciences in Glasgow, Uk; used multiple enzymes to see what effects they had on the biofilms of both Candida albicans and Candida tropicalis.

Beta-glucanase more easily detached Candida albicans biofilms from plastic surfaces. Protease, the cellulases, and glucoamylase partially detached the biofilm. Candida tropicalis biofilms were only affected by lipase and the chitinases. They also noted that the biofilms definitely contributed to increased drug resistance.(6)

A 2017 study done at the Medical University in Vienna, Austria on the biofilms of Candida albicans using beta-glucanase only; had no effect on its growth but reduced the biofilm by 56%. This greatly enhanced the ability of Fluconazole and Amphotericin B to clear the infection.(7)

The same doctors in Vienna ran another study to monitor the effects of beta-glucanase on the biofilms of Candida tropicalis, Candida parapsilosis and Candida krusei. They observed a reduction in the biofilm of 60%, which greatly enhanced the effects of Amphotericin B. The enzyme had no effect on these species of yeast growth characteristics.(8)

Enzyme Effects on Bacterial Biofilms?

This study done by Loiselle M, Anderson KW at the Department of Chemical and Materials Engineering, University of Kentucky, on the biofilm of the pathogenic bacteria Pseudomonas aeruginosa using the cellulase enzyme, showed a marked reduction in the film. The authors noted that using additional enzymes with the cellulase would probably increase the effectiveness, which is what we have suggested all along.

In 2011, the Max Bergmann Center of Biomaterials in Dresden Germany did a study on the biofilms of Pseudomonas aeruginosa and Staphylococcus epidermidis. They used glycoside hydrolase's, which include the enzymes cellulase, hemicellulase, and amylase. They also used subtilisin A, which is a protease enzyme derived from the bacteria Bacillus subtilis.

They observed that cellulase reduced the biofilm of Staphylococcus epidermidis by 67% while having no effect on the biofilm of Pseudomonas aeruginosa. The protease enzyme had the opposite effect, it had no effect on the biofilm of Staphylococcus epidermidis but reduced the biofilm of Pseudomonas aeruginosa by 44%.(9)

A 2013 study on the bacteria Burkholderia cepacia that typically infects people with medical implants, was done at the Department of Microbiology, PRIST University in India. They used the cellulase enzyme and noted "significant anti-biofilm activity".(10)

In 2017, a study was performed at the University of Porto in Portugal on the biofilms of the pathogenic bacteria Pseudomonas fluorescens. The enzyme beta-glucanase, amylase, lipase and protease were used both by themselves and in combination. A modest removal of the biofilm was observed with protease having the greatest long term effects.(11)

Another 2017 study done at Institute of Fundamental Medicine and Biology in Russia, tested protease on the biofilms of the Staphylococcus aureus and Staphylococcus epidermidis bacteria. Biofilm thickness decreased 200% within 24 hours of exposure to the protease. The amount of antibiotics then needed to clear the bacteria decreased three fold.(12)

Dr. Vibhuti Rana says...

By now, it is quite clear that a biofilm provides a three-dimensional shield to the cells inside it, be it bacterial, fungal or viral. The chief requirement is to remove or disperse these biofilms using enzymes that are best suited for this job.

Reports have revealed that bacterial polysaccharides are alginate (by Pseudomonas aeruginosa) and poly β 1, 6-linked N-acetylglucosamine (produced by S. epidermidis and S. aureus). This report conducted enzymatic degradation assay on C. albicans and C. tropicalis biofilm matrix using eight different enzymes. Resultantly, it was seen that proteinase K, chitinase, DNase I or β-N-acetylglucosaminidase enzymes were able to partially degrade matrix material, leading to biofilm detachment from the cell surfaces. The enzyme lyticase exhibited the greatest effect, causing an 85 % reduction in optical density of the biofilm (1)

In another study, the enzymes lyticase and beta-glucosidase have been shown to significantly remove Pseudomonas aeruginosa bacterial biofilms, with causing any toxic side-effects in host. (2) In Staphylococcus aureus forming biofilms, enzyme debridement has been reported using enzymatic agents such as papain/urea, bromelain, DNase I/fibrolysin, krillase, dispersin, Proteinase-K, sutilains, and collagenase. (3)

1. Biofilm matrix of Candida albicans and Candida tropicalis: chemical composition and role in drug resistance Journal of Medical Microbiology (2006), 55, 999–1008
2. Banar, M., Emaneini, M., Beigverdi, R. et al. The efficacy of lyticase and β-glucosidase enzymes on biofilm degradation of Pseudomonas aeruginosa strains with different gene profiles. BMC Microbiol 19, 291 (2019).
3. Watters CM, Burton T, Kirui DK, Millenbaugh NJ. Enzymatic degradation of in vitro Staphylococcus aureus biofilms supplemented with human plasma. Infect Drug Resist. 2016;9:71–78. Published 2016 Apr 27. doi:10.2147/IDR.S103101.

Do the Enzymes Work on the Fibrinogen and Fibronectin in the Yeast Biofilm? 

Dr. Atmika Paudel says, "Microorganisms such as bacteria and yeast use fibrinogen and fibronectin to adhere and make biofilms with the help of fibronectin binding proteins present in these microorganisms."

Besides being a very good anti-inflammatory agent, serratiopeptidase literally eats these substances which are basically scar tissue.

Because this enzyme digests non-living tissue and leaves live tissue alone; it has been found to be effective in removing the deposits of fatty substances, cholesterol, cellular waste products, calcium and fibrin on the inside of the arteries. The fibrinolytic clot removing activity of serratiopeptidase may also be able to help with thickened blood, increased risk of stroke, and phlebitis/thrombophlebitis.

It's been reported to have an effect on sinusitis and bronchitis, atherosclerosis, carpal tunnel syndrome, rheumatoid arthritis and other autoimmune diseases.

Serrapeptase effects on biofilms

A 1993 study on prosthetic joints infected by Pseudomonas aeruginosa and Staphylococcus epidermidis, found that serrapeptase greatly enhanced the activity of the antibiotic ofloxacin against these pathogens by inhibiting and removing biofilm formation.(13)

A 2008 study that was published in Microbial Pathogenisis was done on the pathogenic bacteria Listeria monocytogenes, which is a bacteria that causes food poisoning, found that serratiopeptidase sharply reduced the bacteria's ability to form biofilms and attach itself to the human gut.(14)

Serrapeptase has been shown to inhibit fibrin from growing and becoming problematic in an induced animal model, which enhanced the penetration of antibiotics to sites of infection.(15)

In another study, five different protease enzymes were tested on Staphylococcus aureus and Staphylococcus epidermidis bacteria strains for their antimicrobial efficiency. Some proteases showed a nonspecific and indiscriminate effect on the proteins in the biofilm, while others induced a discrete and reproducible action on the proteins. The study concluded that serratiopeptidase, can interfere with adhesion and invasion of eukaryotic cells and biofilm formation.(16)

The ability of serrapeptase to inhibit Staphylococcus aureus's ability to invade human tissues and to adhere to prostheses, catheters and medical devices was proven again in a separate 2013 study.(17)

In 2006, Serratiopeptidase was effective for eradicating infection caused by biofilm-forming bacteria in an experimental animal model.(18)

In spite of being in use for decades, serrapeptase has not been given GRAS status by the FDA but is licensed for use as a natural health product by Health Canada.

I could go on and on here folks but I think at this point, you get it. Especially when you consider these enzymes have been studied repeatedly, and have been found to be effective, since 1968.

 
What have we learned from these biofilm studies?

  • No single enzyme works on the biofilms of every species of candida or bacteria.
  • Using multiple enzymes at once enhances the biofilm removing effects.

  • Once the biofilm is lessened or removed, medications are much more effective. If you were taking prescription drugs such as Fluconazole, these enzymes would enhance its effects. 

  • If medications are more effective after biofilm removal, the appropriate herbs or probiotics would be as well.

  • After the biofilm has been reduced or removed, the enzymes don't always kill the yeast and definitely not bacteria. That means the best thing to do is to take things that will with these enzymes.

What's the Best way to take these enzymes? See our 3-Step Treatment Plan here.

Dr. Atmika Paudel says...

I have already given my commentary regarding yeast enzyme Biofase and others. This is a similar article that talks about the yeast enzyme components and their respective roles.

An article that was published in 2012 in Current Opinion in Microbiology gives a detail information about how a commensal Candida can turn into a pathogen and how its cell structure help it in this transition to establish infection and express virulence factors.(1)

There is a paper published in 2018 in Genome Biology and Evolution that details about a hypervirulent strain of Candida and its genomic comparison with other Candida to give an idea about its evolution. It has been shown that the particular strain harbors many genes related to pathogenesis.(2)

1. Current Opinion in Microbiology, Volume 15, Issue 4, August 2012, Pages 406-412. Importance of the Candida albicans cell wall during commensalism and infection.
2. Suresh Panthee, Hiroshi Hamamoto, Sanae A Ishijima, Atmika Paudel, Kazuhisa Sekimizu, Utilization of Hybrid Assembly Approach to Determine the Genome of an Opportunistic Pathogenic Fungus, Candida albicans TIMM 1768, Genome Biology and Evolution, Volume 10, Issue 8, August 2018, Pages 2017–2022

Final Commentary by Dr. Vibhuti Rana

The information in the article written above explaining the biofilm structures and the importance of enzymes for biofilm degradation is correct.

As we have already come to know, biofilms provide a 3-dimensional surface covering mesh comprising of extra cellular matrix and all macromolecules like proteins, carbohydrates, lipids, and nucleic acids. The Candida yeast biofilm requires both yeast-form and hyphal form. The cohesion builds up with gradual accumulation of extracellular matrix, once the adhesion, cell multiplication, and hyphal induction steps are completed. (1) The fungal mass caused by Aspergillus spp is known as Aspergilloma, and reach mature stage within 24 hours. (2)

Definitely, as Dan writes, a cocktail or a combination of different biofilm-digesting enzymes work best to dilute the density of the biofilm; upon which, suitable anti-fungal treatment is required to accelerate the process of decontamination.

The serratiopeptidase metalloprotease enzyme that belongs to trypsin family has been long known for its anti-infective properties. It is a potent anti-inflammatory agent used for treatment of various disorders like bronchitis, arthritis, sinusitis, carpal-tunnel syndrome, etc. (3) However, literature also reveals that they have been used to block biofilm formation and the colonization of S. aureus. (4)

1. Fanning S, Mitchell AP (2012) Fungal Biofilms. PLoS Pathog 8(4): e1002585. Published: April 5, 2012    https://doi.org/10.1371/journal.ppat.1002585 https://doi.org/10.1371/journal.ppat.1002585.
2. Costa-Orlandi CB, Sardi JCO, Pitangui NS, et al. Fungal Biofilms and Polymicrobial Diseases. J Fungi (Basel). 2017;3(2):22. Published 2017 May 10. doi:10.3390/jof3020022
3. The role of serratiopeptidase in the resolution of inflammation. Asian Journal of Pharmaceutical Sciences. Volume 12, Issue 3, May 2017, Pages 209-215
4. Serratiopeptidase: a well-known metalloprotease with a new non-proteolytic activity against S. aureus biofilm. BMC Microbio. 2015.


Updated 1/16/2020

What enzyme for yeast brands are the best to use? See our review here

Yeast Infection Advisor Home

If you have any questions about these enzymes for yeast infection please feel free to contact us from the contact page of this website.

Article References

1. Journal of General Microbiology (1980), 119, 341-349. Printed in Great Britain 341 Protoplasts from Yeast and Mycelial Forms of Candida albicans
2. Journal of General Microbiology (1976), 95,335-347 Printed in Great Britain 335 Changes in the Cell Surface of the Dimorphic Forms of Candida albicans by Treatment with Hydrolytic Enzymes.
3. Journal of General Microbiology (1980), 117, 383-391. Printed in Great Britain Reduction of Amphotericin Resistance in Stationary Phase Cultures of Candida albicans by Treatment with Enzymes
4. Yeast. 2003 Jan 15;20(1):25-30. Real-time imaging of the surface topography of living yeast cells by atomic force microscopy.
5. Microb Pathog. 2017 Sep;110:159-164. doi: 10.1016/j.micpath.2017.06.038. Epub 2017 Jun 28. Antifungal activity and expression patterns of extracellular chitinase and β-1,3-glucanase in Wickerhamomyces anomalus EG2 treated with chitin and glucan.
6. J Med Microbiol. 2006 Aug;55(Pt 8):999-1008. Biofilm matrix of Candida albicans and Candida tropicalis: chemical composition and role in drug resistance.
7. Int J Biol Macromol. 2018 Mar;108:942-946. doi: 10.1016/j.ijbiomac.2017.11.003. Epub 2017 Nov 4. β-1,3-glucanase disrupts biofilm formation and increases antifungal susceptibility of Candida albicans DAY185.
8. Microb Pathog. 2017 Dec;113:342-347. doi: 10.1016/j.micpath.2017.10.057. Epub 2017 Nov 1. Dispersal of single and mixed non-albicans Candida species biofilms by β-1,3-glucanase in vitro. https://www.ncbi.nlm.nih.gov/pubmed/29101060
9. Biotechnol Lett. 2011 Sep;33(9):1897-904. doi: 10.1007/s10529-011-0643-3. Epub 2011 May 27. Immobilized enzymes affect biofilm formation. https://www.ncbi.nlm.nih.gov/pubmed/21618024
10. Pol J Microbiol. 2013;62(3):327-30. Cellulase inhibits Burkholderia cepacia biofilms on diverse prosthetic materials. https://www.ncbi.nlm.nih.gov/pubmed/24459841
11. Food Res Int. 2017 May;95:101-107. doi: 10.1016/j.foodres.2017.02.016. Epub 2017 Feb 28. Combination of selected enzymes with cetyltrimethylammonium bromide in biofilm inactivation, removal and regrowth. https://www.ncbi.nlm.nih.gov/pubmed/28395817
12. Sci Rep. 2017 Apr 7;7:46068. doi: 10.1038/srep46068. Targeting microbial biofilms using Ficin, a nonspecific plant protease.
13. Selan L, Berlutti F, Passariello C, Comodi-Ballanti MR, Thaller MC. Proteolytic enzymes: a new treatment strategy for prosthetic infections? Antimicrob Agents Chemother. 1993;37(12):2618-2621.8109925
14. Longhi C, Scoarughi GL, Poggiali F, et al. Protease treatment affects both invasion ability and biofilm formation in Listeria monocytogenes. Microb Pathog. 2008;45(1):45-52.18479885
15. Kakinuma A, Moriya N, Kawahara K, Sugino H. Repression of fibrinolysis in scalded rats by administration of Serratia protease. Biochem Pharmacol. 1982;31(18):2861-2866.6753849
16. Artini M, Papa R, Scoarughi GL, et al. Comparison of the action of different proteases on virulence properties related to the staphylococcal surface. J Appl Microbiol. 2013;114(1):266-277.23057709
17. Papa R, Artini M, Cellini A, et al. A new anti-infective strategy to reduce the spreading of antibiotic resistance by the action on adhesion-mediated virulence factors in Staphylococcus aureus. Microb Pathog. 2013;63:44-53.23811076
18. Mecitoglu M, Saygi B, Yildirim Y, Karadag-Saygi E, Ramadan SS, Esemenli T. The effect of proteolytic enzyme serratiopeptidase in the treatment of experimental implant-related infection. J Bone Joint Surg Am. 2006;88(6):1208-1214.16757752

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