For the millions of people who take anti-inflammatory medications to relieve pain and promote cardiovascular health, there is a natural alternative that has now been proven to be very effective. Serrapeptidase is an enzyme that is produced in the intestines of silk worms to break down cocoon walls, and is processed commercially today through a fermentation process.
Doctors in Europe and Japan have been prescribing serrapeptidase for over 20 years to treat everything from pain to atherosclerotic plaques. It has gained a reputation as a potent analgesic and anti-inflammatory, and is used as an effective alternative to aspirin, ibuprofen, and prescription NSAIDs. And unlike these drugs, serrapeptidase is a naturally occurring, physiologic agent that has no gastrointestinal side effects.
NSAIDs is an acronym for “Non-Steroidal Anti-Inflammatory Drugs”, which have traditionally been used to treat pain, inflammation, rheumatoid arthritis and osteoarthritis. Non-selective (COX-1 and COX-2) NSAIDs include Ibuprofen, Acetaminophen, and salicylates (Aspirin). Selective NSAIDs include COX-2 inhibiting products, such as the popular drugs that have recently been taken off the market due to their damaging side effects.
With the recent reports linking COX-2 inhibitors to heart attacks, strokes, intestinal bleeding, kidney or liver impairment, and respiratory infections, people are demanding a safe, natural alternative that is effective.
Serrapeptidase may well be the answer.
The nature of protein dissolving enzymes
Serrapeptidase is a proteolytic (literally, “protein-dissolving”) enzyme, capable of chopping up and digesting non-living tissue such as blood clots, cysts, arterial plaque and inflammation in all forms.
Proteolytic enzymes (also known as proteinases or peptidases) are ubiquitous in nature, being found in animals, plants, bacteria, and fungi. Human beings produce such well-known peptidases as trypsin and chymotrypsin to help digest food, and also generate countless others to control virtually every regulatory mechanism in our bodies.
For example, various peptidases are involved in initiating blood clotting (thrombogenesis) and also in dissolving clots (fibrinolysis); in evoking an immune response and quelling it; and in both promoting and halting inflammation. The mechanism in each case is the ability of the enzyme to cut a protein target into two or more pieces, usually at very specific sites.
It is thought that the analgesic effect of proteolytic enzymes is due to their cutting of bradykinin, a messenger molecule involved in pain signaling. Many studies of proteolytic enzymes over the years have demonstrated their effectiveness in relieving pain and inflammation independently of steroids or NSAIDs.
The medical use of enzymes as anti-inflammatory agents goes back many years. In the early 1950s it was discovered that intravenous trypsin could relieve the symptoms of many different inflammatory conditions, including rheumatoid arthritis, ulcerative colitis, and atypical viral pneumonia. Subsequently, intramuscular enzyme injections were found to be beneficial in counteracting post-surgical swelling (edema), treating thrombophlebitis and lower back strain, and rapidly healing bruises caused by sports injuries.
Around 35 years ago researchers found that if the protolytic enzyme was enterically-coated, it could be taken orally. This enteric coating allows the enzyme to be released in the intestines (where it can be absorbed) and not in the stomach (where it gets digested). The proteolytic enzymes commonly used today derive from bacteria (serrapeptidase grown from serratia cultures), plants (bromelain from pineapple stem and papain from papaya), and animal sources (trypsin and chymotrypsin from hogs or cattle).
Although they can all be useful, serrapeptidase has been shown to provide the greatest benefits in a wide range of applications.
For example, in a study comparing serrapeptidase to trypsin, chymotrypsin, and pronase (another microbial peptidase), serrapeptidase was shown to be far more effective than the other enzymes in repressing fibrinolysis, in agreement with its documented clinical efficacy as an anti-inflammatory agent.