Subtilisin NAT
Crystal structure of nattokinase. PDB 4dww[1]
Identifiers
OrganismBacillus subtilis natto
SymbolaprN
UniProtP35835
Other data
EC number3.4.21.62
Search for
StructuresSwiss-model
DomainsInterPro

Nattokinase (pronounced nuh-TOH-kin-ayss) is an enzyme extracted and purified from a Japanese food called nattō. Nattō is produced by fermentation by adding the bacterium Bacillus subtilis var natto, which also produces the enzyme, to boiled soybeans. While other soy foods contain enzymes, it is only the nattō preparation that contains the specific nattokinase enzyme.

In spite of its name, nattokinase is not a kinase enzyme (and should not be pronounced as such), but a serine protease of the subtilisin family (99.5% identical with aprE). Rather, it is named for the fact that it is an enzyme produced by nattōkin (納豆), the Japanese name for Bacillus subtilis var natto. When in contact with human blood or blood clots, it exhibits a strong fibrinolytic activity and works by inactivating plasminogen activator inhibitor 1 (PAI-1).[2][3][4][5] Although it should be expected to be digested and inactivated in the human gut like other proteins, a few researchers report that nattokinase is active when taken orally.[6]

Nattokinase is sold as a dietary supplement. It can now be produced by recombinant means[7][8] and in batch culture,[9][10] rather than relying on extraction from nattō.

See also

References

  1. Yanagisawa Y, Chatake T, Chiba-Kamoshida K, Naito S, Ohsugi T, Sumi H, et al. (December 2010). "Purification, crystallization and preliminary X-ray diffraction experiment of nattokinase from Bacillus subtilis natto". Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 66 (Pt 12): 1670–3. doi:10.1107/S1744309110043137. PMC 2998380. PMID 21139221.
  2. Urano T, Ihara H, Umemura K, Suzuki Y, Oike M, Akita S, et al. (July 2001). "The profibrinolytic enzyme subtilisin NAT purified from Bacillus subtilis Cleaves and inactivates plasminogen activator inhibitor type 1". The Journal of Biological Chemistry. 276 (27): 24690–6. doi:10.1074/jbc.M101751200. PMID 11325965.
  3. Fujita M, Nomura K, Hong K, Ito Y, Asada A, Nishimuro S (December 1993). "Purification and characterization of a strong fibrinolytic enzyme (nattokinase) in the vegetable cheese natto, a popular soybean fermented food in Japan". Biochemical and Biophysical Research Communications. 197 (3): 1340–7. doi:10.1006/bbrc.1993.2624. PMID 8280151.
  4. "Can You Take Nattokinase With Coumadin (Warfarin)?". PharmacistAnswers. Retrieved 2019-02-20.
  5. Sumi H, Hamada H, Tsushima H, Mihara H, Muraki H (October 1987). "A novel fibrinolytic enzyme (nattokinase) in the vegetable cheese Natto; a typical and popular soybean food in the Japanese diet". Experientia. 43 (10): 1110–1. doi:10.1007/bf01956052. PMID 3478223. S2CID 13476341.
  6. Chen H, McGowan EM, Ren N, Lal S, Nassif N, Shad-Kaneez F, et al. (2018). "Nattokinase: A Promising Alternative in Prevention and Treatment of Cardiovascular Diseases". Biomarker Insights. 13: 1177271918785130. doi:10.1177/1177271918785130. PMC 6043915. PMID 30013308.
  7. Liang X, Jia S, Sun Y, Chen M, Chen X, Zhong J, Huan L (November 2007). "Secretory expression of nattokinase from Bacillus subtilis YF38 in Escherichia coli". Molecular Biotechnology. 37 (3): 187–94. doi:10.1007/s12033-007-0060-y. PMID 17952663. S2CID 11595829.
  8. Li X, Wang X, Xiong S, Zhang J, Cai L, Yang Y (October 2007). "Expression and purification of recombinant nattokinase in Spodoptera frugiperda cells". Biotechnology Letters. 29 (10): 1459–64. doi:10.1007/s10529-007-9426-2. PMID 17581705. S2CID 26608552.
  9. Cho YH, Song JY, Kim KM, Kim MK, Lee IY, Kim SB, et al. (September 2010). "Production of nattokinase by batch and fed-batch culture of Bacillus subtilis". New Biotechnology. 27 (4): 341–6. doi:10.1016/j.nbt.2010.06.003. PMID 20541632.
  10. Kwon EY, Kim KM, Kim MK, Lee IY, Kim BS (September 2011). "Production of nattokinase by high cell density fed-batch culture of Bacillus subtilis". Bioprocess and Biosystems Engineering. 34 (7): 789–93. doi:10.1007/s00449-011-0527-x. PMID 21336955. S2CID 38816306.
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