Laboratory Studies on Nattokinase and Abnormal Protein Aggregates

This article was updated with audio on August 15, 2025.

This article discusses research that has shown nattokinase can dissolve amyloid and prion proteins.

What are Amyloids and Prions?

Both are abnormal proteins because they are misfolded. Proteins in various parts of the body serve multiple functions. Proteins can be structural (bone), related to movement (muscles), and protection (skin).

Proteins are also found in hormones, such as insulin, digestive enzymes, cytokines, and blood cells that are responsible for the immune response.

Proteins have to be in a proper shape to be functional. If not, they could cause diseases.

Amyloids

Amyloids can be found in the brains of people with neurodegenerative conditions like Alzheimer’s, Parkinson’s, and Huntington’s disease.

Amyloid-beta (Aβ) fibril accumulation in the brain is associated with Alzheimer’s disease. The alpha-synuclein protein is found in Lewy Body Dementia and Parkinson’s Disease.

Amyloids are also associated with type 2 diabetes and spongiform encephalopathies, characterized by holes in the brain that resemble a sponge.

The list below shows some amyloid proteins and their respective precursors, as well as the diseases they cause.[2]  The precursor proteins are the commonly occurring functional proteins. Once misfolded, they become amyloids and cause illness.

Prions

A prion is a misfolded protein that can spread to others. They are found in animals and humans. Examples are scrapie in sheep, chronic wasting disease in deer, and bovine spongiform encephalopathy (BSE) in cattle (commonly known as “mad cow disease”).

In humans, prions cause Jacob-Creutzfeldt Disease (CJD), the human version of mad cow disease. It is believed that CJD is caused by ingesting beef with prions from a “mad cow.”

The image below is a microscopic view of a brain with spongiform degeneration in a patient who died of Creutzfeldt-Jakob disease (CJD).

Source: By Tulemo – Own work, CC BY-SA 4.0, https://commons.wikimedia.org/w/index.php?curid=119745241

CJD after the COVID shots

In a preprint study that included the late Nobel Prize-winning virologist Luc Montagnier as one of the authors, they reported 26 cases of new-onset CJD after their COVID jabs.

Twenty-three out of the 26 cases developed symptoms within 15 days of their second injection of an mRNA vaccine. The other three cases were associated with AstraZeneca, a DNA vector vaccine, and symptoms appeared within the first month. The time to death was under five months after the injection.

Twenty-three out of the 26 cases developed symptoms within 15 days of their second injection of an mRNA vaccine.

Prions are considered a subclass of amyloid. Research on amyloids and prions is ongoing, and the more we know, the more the lines between amyloids and prions are blurred.

“A preprint describing several CJD cases after vaccination has circulated widely. Because this study has not undergone peer review and observational reports cannot establish cause and effect, these findings should be interpreted with caution.”

Endogenous prions. Not all people with CJD got it from a “mad cow.” Prions can also form inside the body from human proteins. A review article listed 37 peptides or proteins that can form extracellular amyloid deposits in human diseases.[3]

There are other ways to get infected with prion diseases: blood transfusion [4] and contaminated surgical instruments. In 2016, Maine Medical Center postponed all its elective surgeries as a precaution when one patient was diagnosed with a possible prion disease.

In summary, prions and amyloid-related diseases are not that rare and may be more common than we know. It can spread by blood transfusion, contaminated surgical instruments, or form spontaneously inside the body.

Is there a solution?

Nattokinase can degrade amyloid and prions

One study might provide an answer. The study Amyloid-Degrading Ability of Nattokinase from Bacillus subtilis Natto was published in the Journal of Agricultural and Food Chemistry.[1]

The study compared the ability of nattokinase and other serine proteases to digest amyloid-beta (Aβ) fibrils, insulin amyloid fibrils, and human prion proteins.

Nattokinase is an enzyme produced by the bacterium Bacillus subtilis. It is commonly found in natto, a fermented soybean food. It is also available over-the-counter.

Best Naturals Nattokinase 2,000 FU (100 mg) 

Amyloid-beta fibrils are one of the major components of amyloid plaques in Alzheimer’s disease.

Insulin fibrils resulting from repeated insulin injections in diabetes patients can cause injection-localized amyloidosis. Insulin fibrils can block insulin pumps.

They found that nattokinase can effectively degrade the three abnormal proteins in a condition mimicking the human body. (physiologic pH of 7 and temperature of 37°C). Additionally, nattokinase was more efficient than plasmin in cleaving amyloid under the same conditions.[1]

Plasmin is a substance typically formed in the human body that dissolves blood clots. The ability of nattokinase to dissolve blood clots makes it an effective thrombolytic agent.

I discussed that in The Outstanding Vascular Effects and Dose of Nattokinase.

The research also found that nattokinase is more efficient in degrading amyloids and prions than other protease enzymes. And nattokinase is the only enzyme that can be taken by mouth and retain its effectiveness.[1]

The ability to degrade amyloids outside the brain is notable because recent studies found that amyloid-beta clearance outside the brain substantially lowers amyloid accumulation in the brain and potentially lower the risk of Alzheimer’s disease.[5]

How This Research Fits Into the Larger Scientific Landscape

Recent studies show that amyloid clearance outside the brain may influence overall brain amyloid burden, suggesting that peripheral mechanisms play a role in neurodegenerative disease progression. The idea that enzymes like nattokinase may contribute to clearance pathways is scientifically plausible and worth exploring further, though it has not been proven in clinical populations

Evidence Summary: What Studies Show About Nattokinase

The key paper reviewed—“Amyloid-Degrading Ability of Nattokinase from Bacillus subtilis Natto”—demonstrated that nattokinase can degrade:

• Amyloid-beta fibrils (linked with Alzheimer’s disease)
• Insulin-derived amyloid fibrils
• Human prion proteins

and does so more efficiently than plasmin, a natural clot-dissolving enzyme in the human body.

These results occurred under physiologic pH (7.0) and body temperature (37°C)—conditions meant to mimic human tissue environments. This type of testing strengthens the plausibility of real-world activity, though clinical trials in humans remain limited.

To conclude, amyloid and prion diseases could be more common than initially thought. Nattokinase could break up amyloid and prion proteins and potentially solve those problems.

Important Distinction: Laboratory Results vs Human Outcomes

While the enzymatic activity of nattokinase is demonstrated in vitro, more research is needed to determine:

• Absorption and bioavailability
• Ability to reach target tissues
• Long-term safety in higher doses
• Whether amyloid/prion reduction happens in actual human disease

These limitations are common in early-stage biochemical research and must be communicated clearly for transparency.

Safety, Limitations, and Responsible Use

Nattokinase is widely available as a supplement, but several cautions apply:

• It has anticoagulant effects and may increase bleeding risk.
• It should be used carefully—if at all—in people taking antiplatelets, anticoagulants, or with bleeding disorders.
• Human trials examining its effects on amyloid or prion diseases are lacking.
• Supplement quality varies across manufacturers.

The findings described in the paper represent promising biochemical data, not established medical treatment.

Practical Takeaways for Readers

• Nattokinase shows amyloid- and prion-degrading activity in laboratory settings.
• It remains experimental for neurodegenerative or prion diseases.
• People interested in supplements should first discuss them with a healthcare provider, especially those taking medications that affect bleeding or clotting.

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 About Dr. Jesse Santiano

As a physician with decades of experience in internal medicine and emergency medicine, I have followed research on protein misfolding disorders—including amyloids and prions—for many years. These conditions involve abnormal protein folding, which leads to toxic aggregates linked with neurodegenerative and systemic diseases. My training allows me to interpret emerging biochemical and enzymatic research and translate it into understandable language for readers seeking to improve their long-term health.

Why This Topic Matters

Misfolded proteins like amyloid-beta, alpha-synuclein, tau, amylin, and prion proteins are increasingly recognized as contributors not only to disorders like Alzheimer’s or CJD, but also to metabolic diseases like type 2 diabetes. Research shows that amyloids can accumulate inside the brain, in the bloodstream, and even at insulin-injection sites, where they can disrupt normal physiology Nattokinase Degrades Amyloids a….

This makes the idea of enzymatic degradation—breaking these proteins down safely—an important area of investigation.

Medical Disclaimer

This article is for educational purposes only and is not medical advice.
It does not diagnose, treat, cure, or prevent any disease. Information about supplements, biochemical research, and laboratory studies is provided for general knowledge and should not replace a consultation with a qualified healthcare professional.

Do not start, stop, or change any medication or supplement—including nattokinase—without speaking to your physician, especially if you take blood thinners or have a bleeding condition.

If you have symptoms of a neurological disorder, prion disease, or any urgent medical condition, seek medical care immediately.

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Related:

1. Prostate and Vascular problems relieved with Nattokinase
2. Should you take nattokinase on an empty stomach?
3. How to stop bleeding if on nattokinase
4. Natto: An application of the 80-20 Rule
5. How I Made and Appreciate Natto
6. Insulin Resistance and Atherosclerosis and the Nattokinase Solution
7. Protective Effects of Nattokinase against Strokes
8. How to dose Nattokinase, Bromelain and NAC
9. High-Dose Nattokinase to Shrink Atherosclerosis and Lower Blood Lipids
10. Nattokinase is Nontoxic with a High Safety Margin
11. The Outstanding Vascular Effects and Dose of Nattokinase
12. Another Study shows Nattokinase can Destroy the S1 Spike Protein
13. Nattokinase Degrades the SARS-CoV-2 Spike Protein
14. Soy Foods Do Not Increase Breast Cancer Risk

References:

1. National Institute on Aging. “What Is Alzheimer’s Disease?” https://www.nia.nih.gov/health/alzheimers.

2. National Institute of Neurological Disorders and Stroke. “Transmissible Spongiform Encephalopathies.” https://www.ninds.nih.gov/health-information/disorders/transmissible-spongiform-encephalopathies.

3. Mayo Clinic. “Creutzfeldt-Jakob Disease.” https://www.mayoclinic.org/diseases-conditions/creutzfeldt-jakob-disease/symptoms-causes/syc-20371226.

4.  Hsu RL, Lee KT, Wang JH, Lee LY, Chen RP. Amyloid-degrading ability of nattokinase from Bacillus subtilis natto. J Agric Food Chem. 2009 Jan 28;57(2):503-8. PMID: 19117402 Doi: 10.1021/jf803072r.
5. Rambaran RN, Serpell LC. Amyloid fibrils: abnormal protein assembly. Prion. 2008 Jul-Sep;2(3):112-7. doi: 10.4161/pri.2.3.7488. Epub 2008 Jul 20. PMID: 19158505; PMCID: PMC2634529.
6. Chiti, F.; Dobson, C. M. Protein misfolding, functional amyloid, and human disease. Annu. ReV. Biochem. 2006, 75, 333–366.
7. Hunter, N.; Foster, J.; Chong, A.; McCutcheon, S.; Parnham, D.; Eaton, S.; MacKenzie, C.; Houston, F. Transmission of prion diseases by blood transfusion. J. Gen. Virol. 2002, 83, 2897–2905.
8. Cheng, Y., Tian, DY. & Wang, YJ. Peripheral clearance of brain-derived Aβ in Alzheimer’s disease: pathophysiology and therapeutic perspectives. Transl Neurodegener 9, 16 (2020). https://doi.org/10.1186/s40035-020-00195-1

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