Component
Heat-inactivated nattokinase
Nattokinase heated until its protease activity is destroyed, at 70 C or above for loss of fibrinolytic and amidolytic activity and at 120-121 C for 15 min in the studies recorded here. It is kept separate from the active enzyme because two of the effects in this chapter belong to it and not to the active protease.
2 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
What it acts on
Culture solutions of Bacillus subtilis natto and market nattokinase, deactivated by heating at 121 C for 15 min, raised tissue-plasminogen-activator activity in HeLa cells about 20-fold and 24-fold and in human umbilical vein endothelial cells about 5-fold.
Experimental context and source evidence
- duration
- Not stated here
- evidence_access
- Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
- experimental_model
- Human cells
- exposure
- Heat-deactivated nattokinase and heat-deactivated B. subtilis natto culture solution
- limitations
- The subject here is the heat-inactivated material, not the active protease: the same report shows that heating to 70 C or above destroys the fibrinolytic and amidolytic activity. Cell counts did not change, so the effect is not a viability artefact. This is a regulated cellular response, not proteolytic generation of tPA, and it conflicts in direction with the endothelial result recorded next.
- organism
- Human cells
- plain_language
- Culture solutions of Bacillus subtilis natto and market nattokinase, deactivated by heating at 121 C for 15 min, raised tissue-plasminogen-activator activity in HeLa cells about 20-fold and 24-fold and in human umbilical vein endothelial cells about 5-fold.
- primary_references
- Nattokinase-promoted tissue plasminogen activator release from human cells. (2008) https://pubmed.ncbi.nlm.nih.gov/19996631/ DOI: 10.1159/000252817
- route
- In vitro
- tissue
- HeLa and human umbilical vein endothelial cells
Nattokinase: what the purified enzyme cleaves, what survives being eaten, and the gap between the two (2026-09-23) · lines 433–433
Original AI-assisted curation built from a supplied entity-first document of 105 entities and 129 claims. Every reference in that document was resolved against live PubMed with its abstract read and its DOI cross-checked on 2026-09-23, and the EFSA novel-food opinion was retrieved and read in full. That check corrected two PMIDs that pointed at unrelated papers, two DOIs, and two papers recorded as carrying no erratum that do carry one; it also reversed three findings the supplied document had stated backwards. Two papers carry a published correction, recorded as such and not as a retraction. Three sources are not indexed in PubMed and are cited by what they have. Laboratory lineages are recorded, so the four papers from one group, the three from another and the two readings of a single applicant dossier cannot be counted as separate lines of support. Study-specific doses, units, populations and limitations retained; activity units are never converted between systems. Not publisher full text. · supports · Human cells · source_derived_draft · unverified_draft
Culture solutions of Bacillus subtilis natto and market nattokinase, deactivated by heating at 121 C for 15 min, raised tissue-plasminogen-activator activity in HeLa cells about 20-fold and 24-fold and in human umbilical vein endothelial cells about 5-fold.
Complete structured claim and evidenceHeat treatment at 120 C for 15 min markedly increased the ACE-inhibitory activity of subtilisin NAT while inactivating it as a protease and fragmenting it into small peptides.
Experimental context and source evidence
- duration
- 15 min heating
- evidence_access
- Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
- experimental_model
- Purified subtilisin NAT
- exposure
- Subtilisin NAT, heat-treated at 120 C for 15 min
- limitations
- This is the clearest evidence in the chapter that destroying the enzyme creates a different pharmacological species rather than nothing. The authors state the inhibition is not due to an enzymatic action of the protease. Inhibition was of mixed type: Vmax fell and Km rose.
- organism
- Purified subtilisin NAT
- plain_language
- Heat treatment at 120 C for 15 min markedly increased the ACE-inhibitory activity of subtilisin NAT while inactivating it as a protease and fragmenting it into small peptides.
- primary_references
- Inhibition of angiotensin I converting enzyme by subtilisin NAT (nattokinase) in natto, a Japanese traditional fermented food. (2012) https://pubmed.ncbi.nlm.nih.gov/22453301/ DOI: 10.1039/c2fo10245e
- route
- In vitro
- tissue
- ACE inhibition assay
Nattokinase: what the purified enzyme cleaves, what survives being eaten, and the gap between the two (2026-09-23) · lines 675–675
Original AI-assisted curation built from a supplied entity-first document of 105 entities and 129 claims. Every reference in that document was resolved against live PubMed with its abstract read and its DOI cross-checked on 2026-09-23, and the EFSA novel-food opinion was retrieved and read in full. That check corrected two PMIDs that pointed at unrelated papers, two DOIs, and two papers recorded as carrying no erratum that do carry one; it also reversed three findings the supplied document had stated backwards. Two papers carry a published correction, recorded as such and not as a retraction. Three sources are not indexed in PubMed and are cited by what they have. Laboratory lineages are recorded, so the four papers from one group, the three from another and the two readings of a single applicant dossier cannot be counted as separate lines of support. Study-specific doses, units, populations and limitations retained; activity units are never converted between systems. Not publisher full text. · supports · Purified subtilisin NAT · source_derived_draft · unverified_draft
Heat treatment at 120 C for 15 min markedly increased the ACE-inhibitory activity of subtilisin NAT while inactivating it as a protease and fragmenting it into small peptides.
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.