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 Amylase enzymes from plant sources are effective in vitro in the treat-
have been documented in numerous research studies. Most of the excite- ment of celiac disease. By enzymatically cleaving the toxic carbohydrate
ment and knowledge of this vital nutritional factor stems back to the portion of gliadin, plant amylase preparations render grains like wheat
work of biochemist, Dr. Edward Howell, whose extensive, pioneering and rye virtually harmless to individuals with gluten enteropathy (16,17).
study into the enzyme concept began more than 50 years ago. His work,
and that of other noted researchers, has shown the benefits of supple- With the prevalence and wide range of documented research, it is obvi-
mental plant enzymes on various conditions of the body, particularly as ous that plant enzymes benefit specific conditions in the body. Much of
they relate to the digestion and assimilation of foods. this research has gone unrecognized by some health care professionals,
particularly the research dealing with the intact absorption of food sub-
Recent research has been increasingly more specific, focusing on different strates. This research proves undoubtedly that non-digested food sub-
types and sources of plant enzymes, including various protease, lipase, strates do enter the blood and that plant enzymes can greatly benefit the
carbohydrase, and cellulase preparations. Both in vitro and controlled in bloodstream by breaking down different food substrates that otherwise
vivo studies using internal and parenteral routes have examined the effec- would pass into the blood without being fully digested. This research
tiveness of these enzymes in a wide range of conditions including supports and is confirmed by the findings of live blood tests before and
maldigestion, malabsorption, pancreatic insufficiency, steatorrhea, celiac after taking pure plant enzymes.
disease, lactose intolerance, arterial obstruction and thrombotic disease.
Reports from doctors across the nation indicate that plant enzymes are Macromolecules can and do pass intact from the human gut into the
being used in an even broader spectrum of clinical conditions. bloodstream under normal conditions (18-23, 25). This has been described as
the "leaky bowel" phenomenon and may help to explain the apparent
Data from various studies and clinical applications verify the efficacy of effectiveness of plant enzyme therapy in the nutritional management of
plant enzymes for a broad spectrum of conditions: conditions, including food allergies, inflammatory bowel disease,
immune dysfunction and certain inflammatory disorders (18, 19, 35-43).
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 conven- Pure plant enzymes (molecular weight approximately 35,000) are fully
tional pancreatin (10,000mg) in the treatment of malabsorption, malnu- absorbed following oral administration. These proteases exhibit the same
trition and steatorrhea due to pancreatic exocrine insufficiency. Unlike properties in the bloodstream as in other applications. This includes the
pancreatin, plant enzyme lipase delivers enzyme activity in the broad pH ability to hydrolyze dietary proteins and polypeptides that have leaked
range from 3 to 9. It safely digests dietary fat in pancreatic insufficient into the bloodstream as food antigens. Protease shows anti-inflammatory
patients, beginning in the stomach and continuing in the abnormal properties (5,8,9,12,14) and has been shown to be effective when administered
acidic conditions commonly found in the duodenum and jejunum. intravenously in re-establishing circulation through chronically obstruct-
ed arteries in humans (4,13).
Human and animal studies have compared the effectiveness of acid-stable
lipase from various fungal species with that of pancreatin in the treat- Other animal and human studies have shown that numerous specific
ment of malabsorption and steatorrhea due to pancreatic insufficiency. whole proteins, including plant and animal enzymes, are absorbed intact
Administered orally at mealtime, plant lipase has been found to be effec- into the bloodstream following oral administration. These include
tive in these conditions and to offer certain advantages of both conven- human albumin and lactalbumin, bovine albumin, ovalbumin, lactoglob-
tional and enteric-coated pancreatic enzyme replacement therapy. ulin, 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
Chronic pancreatitis and cystic fibrosis are the most common causes of inert particles, such as carbon particles from India ink (18), and whole
pancreatic exocrine insufficiency.(1) Pancreatogenic steatorrhea results viruses (26) can cross the healthy intestine.
from failure of fat digestion leading to lipid malabsorption, impaired
nutrition, weight loss and considerable social embarrassment. Proteins and polypeptides absorbed intact from the gut can exert phar-
Protease enzymes dramatically improve chronically obstructed arteries in macological effects on target tissues. Several peptide hormones are known
humans (1,2,3). Numerous crossover, single-blind and placebo studies have to be biologically active when administered orally, including luteinizing
confirmed this (4,5). Intravenous therapy with plant protease is dramatically hormone releasing factor and thyrotropin releasing hormone (27,28).
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).
Page 1 © 2001 Infinity2, Inc. Form #1913 Rev. 04/04/01
Plant Enzyme Therapy and Absorption of Undigested
Food Substrates in the Blood Stream (continued)
Stan Bynum, Ph.D.
Insulin can cross the intestinal mucosa intact and produce significant By digesting dietary protein, plant enzymes administered orally at meal-
hypoglycemia under limited circumstances (e.g. in the presence of pro- time work to decrease the supply of antigenic macromolecules available
tease inhibitors or hypertonic solutions in the intestinal lumen) (29,30). to leak into the bloodstream. In addition, orally administered plant
enzymes, which have, themselves, been absorbed intact, may help to
There is strong evidence that the body seeks to conserve its digestive "digest" antigenic dietary proteins that they encounter in the blood-
enzymes by absorbing intact endogenous and exogenous pancreatic stream. Further research is needed to evaluate the role of plant enzymes
enzymes. Trypsin and chymotrypsin are absorbed intact into the blood in the treatment of food allergies.
stream in an enzymatically active form following oral administration.
Considerable evidence exists supporting the biological and therapeutic
Even more dramatic is the finding that both endogenous and exogenous importance of the "leaky bowel" phenomenon and the role of plant
enzymes are not only absorbed intact from the gut, but also transported enzyme therapy. The intact absorption of orally administered foods and
through the bloodstream, taken up intact by pancreatic secretory cells, plant enzymes can no longer be reasonably denied.
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.
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.
Page 2 For more information: 1-800-255-2430 or www.infinity2.com © 2001 Infinity2, Inc. Form #1913 Rev. 04/04/01