Serrapeptase: Drano for your Vein-o
COVID, vaccine injury, heart disease and gout: another Japanese miracle drug!
After I published the article on ALS, I asked Twitter to take suggestions for the next topic on which I should write. Thank you to @SmallCaps14 who asked that I write about serrapeptase! I was excited to have identified serrapeptase as having a number of useful functions for the treatment of COVID-19, and its utility far exceeds just that. Let’s dive into it…
What is Serrapeptase?
Serrapeptase is a proteolytic enzyme produced by silkworms. Proteolytic is a portmanteau of two words: protein, and lytic, which means “to cut.” The enzyme is produced in the silkworm’s gut by a symbiotic enterobacteria called Serratia E-15. Upon the silkworm’s metamorphosis into a silk moth, the enzyme is used by the silkworm to dissolve the cocoon and free the moth. It is a powerful proteolytic, supplanted perhaps only by lumbrokinase, and it has a host of benefits for human consumption. Especially in the era of chronic COVID and vaccine injury, Serrapeptase is an invaluable tool at our disposal to promote and maintain cardiovascular health. Dosage is uniquely measured; rather than milligrams, ounces, or even international units (IU), the dose is measured in SU, which means - imaginatively enough - Serrapeptase Units. A standard dose can range anywhere from 60,000 to 500,000 SU or more, depending heavily on the purpose for which it is being taken. It is also known as Serrapeptidase and Serratiopeptidase, and comes with a few potential side effects. Let’s dig into it.
History
Serrapeptase was discovered in 1967 by Dr. Yamasaki and Dr. Saeki, two widely reputed Japanese scientists. They were studying various serine proteases for potential anti-inflammatory properties, and the protein, isolated from the gut of the silkworm and initially referred to as TSP, showed some promising results. The enzyme quickly gained broad recognition across Japan, and eventually joined the ranks of the thousands of other miscellaneous supplements known across the world.
The evidence for its efficacy as regards anti-inflammatory activity has been mixed; unlike other more commonly known anti-inflammatory drugs, it has no immunomodulatory effect to directly reduce inflammatory immune signals. Rather, it acts to denature undesirable elements primarily within the cardiovascular system, and also exhibits more general systemic activity. As such, if inflammation is present which can be attributed to such an unwanted guest, a reduction of inflammation may be a useful second-order effect; but it is not the primary action of the protein.
This fundamental misunderstanding of its purpose and activity has lead to a significant under-appreciation for its multitude of applications, and resulted in a number of high-quality trials unfortunately and inaccurately determining that it has no appreciable effect on anything. With that in mind - let’s get into the actual functionality of it.
How It Works
As a proteolytic enzyme, the primary utility of the enzyme is - you guessed it - lysing proteins. It does so in a poorly understood, but very useful manner. Imagine a proteolytic enzyme to be a microscopic little buzzsaw: there are an almost infinite number of such proteins, with wildly varying functions, both good, and very bad, for our health.
Proteolytic enzymes within our cells handle numerous tasks, from disposing of misfolded prion proteins, to degrading viral proteins, to facilitating the final steps of apoptosis, when a cell is too badly damaged to survive and destroys itself. Different proteolytic enzymes are found in snake and spider venom, serving to destroy the victim’s cells; the bacterium responsible for gas gangrene, Clostridium perfringens, causes its destruction via the production of proteolytic enzymes. Proteolysis can either be very useful to us, or deathly dangerous, but it is an essential function of every microbiome currently known to exist.