Nattokinase: New Study Shows Promising Clot-Busting Power
Quick Summary: Researchers found a new way to produce nattokinase, an enzyme found in the Japanese food natto. This new method created nattokinase with potentially stronger clot-busting abilities in lab tests.
What Is Nattokinase?
Nattokinase is an enzyme extracted from natto, a fermented soybean food popular in Japan. It's known for its potential to help break down blood clots. This is why it's often used as a dietary supplement.
New Nattokinase: What The Research Found
Scientists successfully produced nattokinase using a special yeast. The nattokinase made this way showed significantly better clot-dissolving activity in lab tests compared to the nattokinase from the original source.
Study Details
- Who was studied: The study was done in a lab, so it didn't involve people. Instead, they tested the nattokinase's ability to dissolve clots in a controlled environment.
- How long: The experiment itself took place over a few days in the lab.
- What they took: The researchers used different concentrations of the nattokinase enzyme in their tests.
What This Means For You
This research is promising because it suggests a potentially more efficient way to produce nattokinase. This could lead to:
- More affordable supplements: If the new production method is successful, it could lower the cost of nattokinase supplements.
- Potentially stronger supplements: The new nattokinase showed better clot-busting ability in the lab. However, more research is needed to confirm this in humans.
Study Limitations
It's important to remember:
- Lab tests only: The study was done in a lab, not on people. We don't know if the same results would happen in the human body.
- More research needed: This is just the first step. More studies are needed to confirm the safety and effectiveness of this new nattokinase.
- Not a replacement for medical care: Nattokinase supplements should not replace any prescribed medications or treatments for blood clots. Always talk to your doctor.
Technical Analysis Details
Key Findings
This study successfully expressed Bacillus subtilis natto-derived nattokinase (NK) in Pichia pastoris GS115, a yeast-based heterologous system. The recombinant NK exhibited significantly higher thrombolytic activity than NK from the native B. subtilis strain. Quantitative analysis showed the recombinant enzyme achieved a clot-dissolving zone diameter of 15.8 ± 0.4 mm in fibrin plate assays, compared to 10.5 ± 0.3 mm for native NK (p < 0.05). The study concluded that P. pastoris is a viable, high-yield platform for NK production, with potential to reduce manufacturing costs for nutraceutical applications.
Study Design
This was an in vitro laboratory study using molecular biology and enzymatic assays. The methodology involved:
1. Cloning the nattokinase gene (aprN) into P. pastoris GS115 via the pPICZαA vector.
2. Optimizing expression using methanol induction.
3. Purifying recombinant NK via Ni-NTA chromatography.
4. Assessing thrombolytic activity using fibrin plate assays (standardized clot-dissolving test).
Sample size comprised triplicate experimental repeats (n = 3) for all assays. No human or animal subjects were involved; the study focused solely on microbial expression and in vitro enzyme characterization. Duration covered standard lab-scale fermentation (72–96 hours).
Dosage & Administration
Not applicable. This study evaluated enzyme production and activity in a laboratory setting, not human or animal supplementation. No doses were administered to living subjects. The "dosage" context relates solely to in vitro enzyme concentrations used in fibrin plate assays (e.g., 20 μL of purified NK solution per assay well).
Results & Efficacy
Recombinant NK from P. pastoris demonstrated 50.5% higher thrombolytic activity than native NK (15.8 vs. 10.5 mm clot-dissolving zone; p < 0.05). Specific activity was 1,840 ± 40 FU/mg (Fibrinolytic Units per milligram) for recombinant NK versus 1,220 ± 30 FU/mg for native NK. Statistical significance was confirmed via Student’s t-test (p < 0.05), with data reported as mean ± SD. No confidence intervals were provided. Efficacy was strictly measured by in vitro fibrin degradation, not clinical outcomes.
Limitations
Key limitations include:
1. No in vivo validation: Activity was tested only in fibrin plates, not in blood or animal models.
2. Purification challenges: Low yield (0.8 mg/L) after chromatography suggests scalability issues.
3. Lack of comparative data: Did not benchmark against other expression systems (e.g., E. coli).
4. No stability/safety testing: Enzyme stability under physiological conditions and potential immunogenicity were unaddressed.
Future research should assess in vivo efficacy, optimize fermentation for higher yields, and conduct toxicity studies.
Clinical Relevance
This study has indirect implications for supplement users. By demonstrating a potentially cheaper, scalable production method for NK, it could lower costs of commercial supplements. However, no direct health benefits were tested. Users should note:
- Recombinant NK’s in vitro superiority does not equate to enhanced human efficacy.
- Current NK supplements predominantly use B. subtilis-derived enzyme; P. pastoris-produced NK remains experimental.
- Clinical relevance hinges on future in vivo studies confirming safety and bioequivalence. Consumers should prioritize products with verified activity data from human trials, not lab-based production metrics.
Original Study Reference
Heterologous expression of nattokinase from B. subtilis natto using Pichia pastoris GS115 and assessment of its thrombolytic activity.
Source: PubMed
Published: 2021-08-09
📄 Read Full Study (PMID: 34372833)
