Amylase is one of the primary starch-digesting enzymes secreted in the body. It is somewhat unusual in that it is produced not only by the pancreas but also in the mouth as a component of saliva. This form is known as ptyalin (ti´ah-lin), and it begins the enzymatic digestion of starches in the oral cavity as food is chewed and mixed with saliva. This begins the reduction of larger, more complex starches into simpler sugars; however the process is largely arrested as the food enters the more acidic environment of the stomach.
How Does Amylase Work?
Pancreatic amylase goes into action after the partially digested food is emptied into the small intestine and the pH returns to the neutral range. Starches continue to be broken into smaller trisaccharides and disaccharides and possibly even into glucose for energy. The primary type of amylase is known as alpha amylase, which hydrolyses (breaks down) the bonds in long starch or glycogen molecules into smaller chains of glucose called dextrins, which are easier to digest. Amylase is also produced by various bacteria and fungal organisms like Aspergillus oryzae from which it can be isolated for effective, vegan-safe dietary supplements
One of the most important parts of our digestive process occurs in the mouth and the saliva. The enzyme amylase helps to relieve the burden of digestion on the small intestine by breaking down food particles while still in the mouth. If this important enzyme were not excreted in the saliva, the small intestine would have a much harder time breaking down sugars and starches. In this way, amylase helps the entire functioning of the digestive system.
Due to poor dietary habits and age most people become deficient in amylase production and may show some signs of deficiency which may include skin rash, allergies, gas, constipation, mood imbalances, and general digestive upset. What is more, having sufficient amylase activity reduces contributors to some degenerative diseases, as it helps the body digest and excrete dead white blood cells. Without proper amylase activity, irritation can be excessive. Low amylase is also thought to be a factor in a variety of diseases including type II diabetes, blood sugar imbalances, hypoglycemia, carbohydrate and sugar cravings, and many forms of food sensitivities.
The Health Benefits of Amylase
1. May Help Lower Autoimmune Responses
One study on digestive enzymes and autoimmune diseases found that these enzymes could help slow the aggregations of antigens (molecules that trigger immune responses), as well as the resulting tissue damage from the heightened conglomeration of antibodies (immune system proteins that neutralize foreign cells). Some scientists are looking into the strong possibility that enzymes such as amylase can play a role in boosting immunomodulatory activity halting these strong immune states. [2-5]
2. Resistant to Swelling and Redness
Many European research groups are actively studying enzymes such as amylase. Oral enzymes are even being used in European countries as studies show that oral enzymes can be as effective in reducing swelling. Several placebo-controlled comparison studies found that patients with rheumatic diseases taking enzymes experienced some anti-swelling effects. These studies suggest that enzyme preparations can be just as effective as strong drugs, without many of the harmful side effects. [6-9]
3. Compromised Health Support
While not an approved course of action in the United States, enzyme therapy is even being studied in Switzerland for its uses as a supportive therapy of cancer. The amylase enzyme in particular was found to show amazing abilities in inhibiting the growth of tumor cells with metastatic capacities. [10-11] The Swiss research team concluded these astounding results of the study: “Enzyme therapy can reduce the adverse effects caused by radiotherapy and chemotherapy. There is also evidence that, in some types of tumors, survival may be prolonged. The beneficial effect of systemic enzyme therapy seems to be based on its potential to reduce redness.”
4. Lessens Aging Effects
While many scientists disagree on the question of whether or not enzyme production decreases as we age, one laboratory study found that pancreatic amylase decreased by 41% in aging rats. Similarly, a human study done in Argentina found that amylase and lipase secretion decreased in women over 45 years of age, but they actually increased in men of the same age. 
How to Read the Units of Measurement for Amylase
Alpha-amylase is measured by the FCC in DU (Dextrinizing Unit). This is a measure of the hydrolysis of gelatinized starches to dextrins and sugars. One DU is defined as the number of grams of soluble starch dextrinized per hour at 30 degrees Celcius and pH 4.6. The FCC notation stands for Foods Chemical Codex and is a division of USP (United States Pharmacopeia). It sets standards for ingredients. In the case of enzymes, FCC is a standard assay used to accurately determine the activity of enzymes. The current compendium is FCC VI.
Where Can I Find The Best Source of Amylase?
The product VeganZyme® contains a 100% vegan form of Amylase produced by the natural fermentation process of Aspergillus oryzae. It comes from all vegetarian, non-GMO sources, is kosher certified, gluten free, made in the USA, contains no animal product and is completely suitable for vegetarians and vegans. VeganZyme is the most advanced full-spectrum systemic and digestive enzyme formula in the world and is free from fillers and toxic compounds. This formula contains digestive enzymes which help digest fats (lipids), sugars, proteins, carbohydrates, gluten, fruits and vegetables, cereals, legumes, bran, nuts and seeds, soy, dairy and all other food sources. VeganZyme may also be used as a systemic enzyme blend to break down excess mucus, fibrin, various toxins, allergens, as well as excess clotting factors throughout your body.
by Dr. Edward Group DC, NP, DACBN, DCBCN, DABFM
Source: The Health Benefits of Amylase
- Suarez F, Levitt MD, Adshead J, Barkin JS. Pancreatic supplements reduce symptomatic response of healthy subjects to a high fat meal. Dig Dis Sci. 1999 Jul;44(7):1317-21.
- Stauder G, Ransberger K, Streichhan P, Van Schaik W, Pollinger W. The use of hydrolytic enzymes as adjuvant therapy in AIDS/ARC/LAS patients. Biomed Pharmacother. 1988;42(1):31-4.
- Stauder G. Pharmacological effects of oral enzyme combinations. Cas Lek Cesk. 1995 Oct 4;134(19):620-4.
- Nouza K. [Systemic enzyme therapy in diseases of the vascular system]. Bratisl Lek Listy. 1995 Oct;96(10):566-9. Czech.
- Heyll U, Münnich U, Senger V. [Proteolytic enzymes as an alternative in comparison with nonsteroidal anti-inflammatory drugs (NSAID) in the treatment of degenerative and inflammatory rheumatic disease: systematic review]. Med Klin (Munich). 2003 Nov 15;98(11):609-15. Review. German.
- Klein G, Kullich W, Schnitker J, Schwann H. Efficacy and tolerance of an oral enzyme combination in painful osteoarthritis of the hip. A double-blind, randomised study comparing oral enzymes with non-steroidal anti-inflammatory drugs. Clin Exp Rheumatol. 2006 Jan-Feb;24(1):25-30.
- Akhtar NM, Naseer R, Farooqi AZ, Aziz W, Nazir M. Oral enzyme combination versus diclofenac in the treatment of osteoarthritis of the knee–a double-blind prospective randomized study. Clin Rheumatol. 2004 Oct;23(5):410-5. Epub 2004 Jul 24.
- Anon. [Oral enzyme therapy in osteoarthritis of the knee. Proteolytic enzyme are effective with few risks]. MMW Fortschr Med. 2001 Jun 7;143(23):44-6. German.
- Leipner J, Iten F, Saller R. Therapy with proteolytic enzymes in rheumatic disorders. BioDrugs. 2001;15(12):779-89. Review.
- Novak JF, Trnka F. Proenzyme therapy of cancer. Anticancer Res. 2005 Mar-Apr;25(2A):1157-77. Erratum in: Anticancer Res. 2005 May-Jun;25(3c):2599.
- Leipner J, Saller R. Systemic enzyme therapy in oncology: effect and mode of action. Drugs. 2000 Apr;59(4):769-80. Review.
- Greenberg RE, Holt PR. Influence of aging upon pancreatic digestive enzymes. Dig Dis Sci. 1986 Sep;31(9):970-7.
- Tiscornia OM, Cresta MA, de Lehmann ES, Celener D, Dreiling DA. Effects of sex and age on pancreatic secretion. Int J Pancreatol. 1986 Jul;1(2):95-118.