Print a Friendly Version Download Full Version in Adobe Reader

Research Paper

Plant Enzyme Therapy and Absorption of
Undigested Food Substrates in the Blood Stream
Stan Bynum, Ph.D.

The benefits of supplemental plant enzymes on your health and blood have been documented in numerous research studies. Most of the excitement and knowledge of this vital nutritional factor stems back to the work of biochemist, Dr. Edward Howell, whose extensive, pioneering study into the enzyme concept began more than 50 years ago. His work, and that of other noted researchers, has shown the benefits of supplemental plant enzymes on various conditions of the body, particularly as they relate to the digestion and assimilation of foods.

Recent research has been increasingly more specific, focusing on different types and sources of plant enzymes, including various protease, lipase, carbohydrase, and cellulase preparations. Both in vitro and controlled in vivo studies using internal and parenteral routes have examined the effectiveness of these enzymes in a wide range of conditions including maldigestion, malabsorption, pancreatic insufficiency, steatorrhea, celiac disease, lactose intolerance, arterial obstruction and thrombotic disease. Reports from doctors across the nation indicate that plant enzymes are being used in an even broader spectrum of clinical conditions.

Data from various studies and clinical applications verify the efficacy of plant enzymes for a broad spectrum of conditions:

An English study showed a small dose of acid-stable lipase from a plant source (400mg) was as effective as a 25 times larger dosage of conventional pancreatin (10,000mg) in the treatment of malabsorption, malnutrition and steatorrhea due to pancreatic exocrine insufficiency. Unlike pancreatin, plant enzyme lipase delivers enzyme activity in the broad pH range from 3 to 9. It safely digests dietary fat in pancreatic insufficient patients, beginning in the stomach and continuing in the abnormal acidic conditions commonly found in the duodenum and jejunum.

Human and animal studies have compared the effectiveness of acid-stable lipase from various fungal species with that of pancreatin in the treatment of malabsorption and steatorrhea due to pancreatic insufficiency. Administered orally at mealtime, plant lipase has been found to be effective in these conditions and to offer certain advantages of both conventional and enteric-coated pancreatic enzyme replacement therapy.

Chronic pancreatitis and cystic fibrosis are the most common causes of pancreatic exocrine insufficiency.(1) Pancreatogenic steatorrhea results from failure of fat digestion leading to lipid malabsorption, impaired nutrition, weight loss and considerable social embarrassment.

Protease enzymes dramatically improve chronically obstructed arteries in humans (1,2,3). Numerous crossover, single-blind and placebo studies have confirmed this (4,5). Intravenous therapy with plant protease is dramatically more effective than anti-coagulant therapy (e.g. heparin, warfarin) at re-canalizing obstructed arteries and improving blood flow through stenosed arterial segments (4,13,15).

Amylase enzymes from plant sources are effective in vitro in the treatment of celiac disease. By enzymatically cleaving the toxic carbohydrate portion of gliadin, plant amylase preparations render grains like wheat and rye virtually harmless to individuals with gluten enteropathy (16,17).

With the prevalence and wide range of documented research, it is obvious that plant enzymes benefit specific conditions in the body. Much of this research has gone unrecognized by some health care professionals, particularly the research dealing with the intact absorption of food substrates. This research proves undoubtedly that non-digested food substrates do enter the blood and that plant enzymes can greatly benefit the bloodstream by breaking down different food substrates that otherwise would pass into the blood without being fully digested. This research supports and is confirmed by the findings of live blood tests before and after taking pure plant enzymes.

Macromolecules can and do pass intact from the human gut into the bloodstream under normal conditions (18-23, 25). This has been described as the "leaky bowel" phenomenon and may help to explain the apparent effectiveness of plant enzyme therapy in the nutritional management of conditions, including food allergies, inflammatory bowel disease, immune dysfunction and certain inflammatory disorders (18, 19, 35-43).

Pure plant enzymes (molecular weight approximately 35,000) are fully absorbed following oral administration. These proteases exhibit the same properties in the bloodstream as in other applications. This includes the ability to hydrolyze dietary proteins and polypeptides that have leaked into the bloodstream as food antigens. Protease shows anti-inflammatory properties (5,8,9,12,14) and has been shown to be effective when administered intravenously in re-establishing circulation through chronically obstructed arteries in humans (4,13).

Other animal and human studies have shown that numerous specific whole proteins, including plant and animal enzymes, are absorbed intact into the bloodstream following oral administration. These include human albumin and lactalbumin, bovine albumin, ovalbumin, lactoglobulin, ferritin (M.A. 500,000), chymotrsinoge, elastase, and other large molecules, such as botulism toxin (M.W. 1,000,000) (18-20,24,32-34). Even inert particles, such as carbon particles from India ink (18), and whole viruses (26) can cross the healthy intestine.

Proteins and polypeptides absorbed intact from the gut can exert pharmacological effects on target tissues. Several peptide hormones are known to be biologically active when administered orally, including luteinizing hormone releasing factor and thyrotropin releasing hormone (27,28).

Insulin can cross the intestinal mucosa intact and produce significant hypoglycemia under limited circumstances (e.g. in the presence of protease inhibitors or hypertonic solutions in the intestinal lumen) (29,30).

There is strong evidence that the body seeks to conserve its digestive enzymes by absorbing intact endogenous and exogenous pancreatic enzymes. Trypsin and chymotrypsin are absorbed intact into the blood stream in an enzymatically active form following oral administration.

Even more dramatic is the finding that both endogenous and exogenous enzymes are not only absorbed intact from the gut, but also transported through the bloodstream, taken up intact by pancreatic secretory cells, and re-secreted into the intestinal lumen by the pancreas mixed with newly synthesized pancreatic enzymes (31). The existence of this enteropancreatic circulation of proteolytic enzymes is closely analogous to the "recycling" of bile salts by the liver.

By digesting dietary protein, plant enzymes administered orally at mealtime work to decrease the supply of antigenic macromolecules available to leak into the bloodstream. In addition, orally administered plant enzymes, which have, themselves, been absorbed intact, may help to "digest" antigenic dietary proteins that they encounter in the bloodstream. Further research is needed to evaluate the role of plant enzymes in the treatment of food allergies.

Considerable evidence exists supporting the biological and therapeutic importance of the "leaky bowel" phenomenon and the role of plant enzyme therapy. The intact absorption of orally administered foods and plant enzymes can no longer be reasonably denied.

Reference List
1. Griffin, S.M., et al. (1989). Acid resistant lipase as replacement therapy in chronic exocrine insufficiency: a study in dogs. Gut 30:1012-1015.
2. Mackie, R.D., et al. (1981). Malabsorption of starch in pancreatic sufficiency. Gastroenterology 80:1220.
3. DiMango, E.P., et al. (1973). Relations between pancreatic enzyme outputs and malabsorption in sever pancreatic insufficiency. N. Eng. J. Med. 228:813-815.
4. Fitzgerald, D.E., et al. (1979). Relief of chronic arterial obstruction using intravenous brinase. Scand. J. Thor. Cardiovasc. Surg. 13:327-332.
5. Bergkvist, R. and Svard, P.C. (1964). Studies on the thrombolytic effect of a protease from Aspergillus oryzae. Acta Physiol. Scand. 60:363-371.
6. Fitzgerald, D.E. and Frisch, E.P. (1973). Relief of chronic peripheral artery obstruction by intravenous brinase. Irish Med. Ass. 66:3.
7. Lund, F., et al. (1975). Thrombolytic treatment with i.v. brinase in advanced arterial obliterative disease. Angiology 26:534.
8. Verstraefe, M. and Verhaege, R. (1977). Clinical study of brinase, a proteolytic enzyme from Aspergillus oryzae. 19th Congr. Intern. Coll. Angiology. Dublin, Ireland.
9. Kiesslling, H. and Svenson, R. (1970). Influence of an enzyme from Aspergillus oryzae, protease 1, on some components of the fibrinolytic system. Acta Chem Scand. 24:569-579.
10. Frisch, E.P., et al. (1975). Dosage of i.v. brinase in man based on brinase inhibitor capacity and coagulation studies. Angiology 26:557.
11. Roschlau, H.E. and Fisher, A.M. (1966). Thrombolytic therapy with local perfusions of CA-7 (fibrinolytic enzyme from Aspergillus oryzae) in the dog. Angiology 17:670-682.
12. Larson, L.J., et al. (1988). Properties of the complex between alpha-2-macro-globulin and brinase, a proteinase from Aspergillus oryzae with thrombolytic effect. Thrombosis Research 49:55-68.
13. Verhaege, R., et al. (1979). Clinical trial of brinase and anticoagulants as a method of treatment for advanced limb ischemia. Eur. J. Clin. Pharmacol. 16:165-170.
14. Vanhove, P., et al. (1979). Action of brinase on human fibrinogen and plasminogen. Thrombos Haemastas. 42:571-581.
15. Frisch, E. P. and Blomback, M. (1979). Blood coagulation studies in patients treated with brinase. In: Progress in Chemical Fibrinolysis and Thrombolysis. Vol IV, J.F. Davidson (Ed.), Edinburgh: Chuchill-Livingstone. Pp 184-187.
16. Phelan, J.J., et al. (1977). Celiac disease: The abolition of gliadin toxicity by enzymes from Aspergillus niger. Clin. Sci. Molec. Med. 53:35-43.
17. McCarthy, C.F. (1976). Nutritional defects in patients with malabsorption. Proc. Nutr. Soc. 35:37-40.
18. Garner, M.L.G. (1988). Gastrointestinal absorption of intact proteins. Ann. Rev. Nutr. 8:329-350.
19. Gardner, M.L.G. (1984). Intestinal assimilation of intact peptides and proteins from the diet – A neglected field? Biol. Rev. 59:289-331.
20. Washaw, A.L., et al. (1974). Protein uptake by the intestine: Evidence for absorption of intact macromolecules. Gastroenterology 66:987-992.
21. Udall, J.N. and Walker, W.A. (1982). The physiologic and pathologic basis for the transport of macromolecules across the intestinal tract. J. Pediatr. Gastroenterol. Nutr. 1:295-301.
22. Loehry, C.A., et al. (1970). Permeability of the small intestine to substances of different molecular weight. Gut, 11:446-470.
23. Hemmings, W.A. and Williams E.W. (1978). Transport of large breakdown products of dietary protein through the gut wall. Gut 19:715-723.
24. Jacobson, I., et al. (1986). Human beta-lactalbumin as a marker of macromolecular absorption. Gut 27:1029-1034.
25. Menzies, I.S. (1984). Transmucosal passage of inert molecules in health and disease. In: Intestinal Absorption and Secretion, E. Skadhauge and K. Heintze (Eds). MTP Press: Lancaster. Pp 527-543.
26. Wolf, J.L., et al. (1981). Intestinal M cells: A pathway for entry of retrovirus into the host. Science 212:471-472.
27. Ormistron, B.J. (1972). Clinical effects of TRH and TSH after i.v. and oral administration in normal volunteers and patients with thyroid disease. In: Thytropin Releasing Hormone (Frontiers of Hormone Research) Vol 1. R. Hall, et al. (Eds). Karger: Basel. Pp45-52.
28. Amoss, M., et al. (1972). Release of gonadotrophins by oral administration of synthetic LRF or a tripeptide fragment of LRF. J. Clin. Endocrinol. Metab. 35:135-177.
29. Siefert, J., et al. (1975). Mucosal permeation of macromolecules and particles. Science 127:505-513.
30. Laskowski, M., et al. (1958). Effect of trypsin inhibitor on passage of insulin across the intestinal barrier. Science 127:1115-1116.
31. Liebow, C. and Rothman, S.S. (1975). Enteropancreatic circulation of digestive enzymes. Science 189:472-474.
32. Bockman, D.E. and Winborn, W.B. (1966). Light and electron microscopy of intestinal ferritin absorption: Observations in sensitized and non-sensitized hamsters. Anat. Rec. 155:603-622.
33. Andre, C., et al. (1974). Interference of oral immunization with the intestinal absorption of heterologous albumin. Eur. J. Immunol. 4:701-704.
34. Dannaeus, A., et al. (1979). Intestinal uptake of ovalbumin in malabsorption and food allergy in relation to serum IgG antibody and orally administrated sodium chromoglycate. Clin. Allergy 9:263-270.
35. Ferguson, A. and Caldwell, F. (1972). Precipitins to dietary proteins in serum and upper intestinal secretions of celiac children. Br. Med. J. 1:75-77.
36. Husby, S., et al. (1987). Passage of dietary antigens into the blood of children with celiac disease: quantification and size distribution of absorbed antigens. Gut 28:1062-1072.
37. Husby, S., et al. (1986). Passage of undergrade dietary antigen into the blood of healthy adults: further characterization of the kinetics of uptake and the size distribution of the antigen. Scand. J. Immunol. 24:447-455.
38. Walker, W.A. (1975). Antigen absorption from the small intestine and gastrointestinal disease. Pediatr. Clin. North Am. 22:731-746.
39. Hamilton, I., et al. (1985). Small intestinal permeability in dermatological disease. Q.J. Med. 56:599-567.
40. Bjarnason, I., et al. (1984). Intestinal permeability in celiac sprue, dermatitis herpetiformis, schizophrenia and atopic eczema. Gastroenterology 86:1029.
41. Heatley, R.V., et al. (1986). Inflammatory bowel disease. In: Gut Defenses in Clinical Practice. M.S. Losowsky and R.V. Heatley (eds). Churchill-Livingstone, Edinburgh. Pp 225-277.
42. Shorter, R.G., et al. (1972). A working hypothesis for the etiology and pathogenesis of nonspecific inflammatory bowel disease. Am. J. Dig. Dis. 17:1024-1032.
43. Jackson, P.G., et al. (1981). Intestinal permeability in patients with eczema and food allergy. Lancet 1:1285-1286.

Special Recognition to Dr. Resnik whose studies contributed to this research.

© 2001 Infinity2, Inc. Form #1914 Rev. 04/04/01



Home | Product Info | CAeDS | Education | Technical Bulletins | Research Papers | FAQ'S | Contact Us

The statements made on Infinity2.net have not been evaluated by the Food and Drug Administration.
The Infinity2 products are not intended to diagnose, treat, cure or prevent any disease.
Legal Notice...