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February 2, 2015 Puzzle Piece - Why Plant Enzyme Therapy Is EXTREMELY Important No Matter the Condition or Diagnosis!

February 2, 2015 Puzzle Piece  


Why Plant Enzyme Therapy Is EXTREMELY Important No Matter the Condition or Diagnosis!

Plant Enzyme Therapy allows better digestion, absorption and utilization.  This prevents many undigested food substrates from entering the bloodstream causing autoimmune reactions!  Remember 80-85% of the Immune System is in the Gut.  Consider increasing its effectiveness by 300% by pre-digestion and using whole food nutrients.

Research Paper By Douglas D. Grant, owner of Optimal Health Systems (OHS).

The benefits of supplemental plant enzymes on your health and blood have been documented in numerous research studies. Our 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.

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 plant sources (400 mg) was as effective as a 25 times larger dosage of conventional pancreatin (10,000 mg) 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 fat in pancreatic insufficiency 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 over 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, malabsorption, impaired nutrition, weight loss and considerable social embarrassment. The OHS products that contain a large amount of lipase are “Digestion” and “Fat-Sugar-Trim”.  The Fat-Sugar-Trim formula is reported to be used extensively in between meals for blood fat issues like high cholesterol and digesting body fat stores.  It is taken with meals when an occoasional cheat meal is consumed that might have processed or fried fats.

Protease enzymes dramatically improve chronically obstructed arteries in humans. (1, 2, 3) Numerous cross-over, 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) Proteases and Peptidase are found both in the “Digestion” and “Acute” formulas.  The Digestion formula is taken with meals to digest the foods being consumed and in-between meals to help break down undigested food substrates that entered the system.  Acute is mainly utilized by professional teams and health practitioners as a natural anti-inflammatory in place of NSAIDS.

Amylase enzymes from plant source 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. (10, 17) The “Digestion” formula has the most balanced and potent forms of Amylase enzymes including the di-saccharide digestion enzymes also.
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 passed into the blood without being fully digested.

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, immune dysfunction and certain inflammatory bowel disease. (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 which 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), chymotrypsinogen, elastase, and other large molecules, such as botulism toxin (M. 1,000,000). (18-20, 24, 32-34) Even inert particles, such as carbon particles from India ink, (and whole viruses (26) can cross the healthy intestine.

Proteins and polypeptide's 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 and is absorbed intact into the bloodstream in an enzymatically active form following oral administration.

Even more dramatic is the finding that both endogenous and exogenous pancreatic 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, co- 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, by themselves, been absorbed intact may help to "digest" antigenic dietary proteins which they encounter in the bloodstream. Further research is needed to evaluate the role of plant enzymes in the treatment of food allergies.

The considerable 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. The most important use of plant enzymes is to take them with meals to digest our food so that there are no macromolecules of food to be absorbed past a leaky gut.  Taking the Digestion enzymes in-between meals has been proven to digest out these possible auto-immune causing food substrates.  Utilizing plant enzymes in your clinics can be one of the greatest tools used to help your patients reach optimal health.

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2. Mackie, R D., et al, Malabsorption of starch in pancreatic sufficiency, Gastroenterology, 80:1220, 1981
3. DiMagno, E. P., et al, Relations between pancreatic enzyme outputs and malabsorption in severe pancreatic insufficiency, N. Eng. J. Med.,     228:813-815, 1973
4. Fitzgerald, D. E., et al Relief of chronic arterial obstruction using intravenous brinase, Scand. J. Thor. Cardiovasc. Surg., 13:327-332,1979.
5. Bergkvist, R and Svard, P. C., Studies on the thrombolytic effect of a protease from Aspergillus oryzae, Acta Physiol.. Sand., 60:363-371,1964
6. Fitzgerald, D. E., and Frisch, E. P., Relief of chronic peripheral artery obstruction by intravenous brinase, Irish Med. Ass., 66:3, 1973.
7. Lund, F., et al, Thrombolytic treatment with i. v. brinase in advance arterial obliterative disease, Angiology, 26:534, 1975.
8. Verstraefe, M. and Verhaege, R, Clinical study if brinase, a proteolytic enzyme from Aspergillus oryzae, 19th Annual Congr. Intern,. Coll.     Angiology, Dublin, Ireland, 1977.
9. Kiesslling, H. and Svenson, R, Influence of an enzyme from Aspergillus oryzae, Protease 1, on some components of the fibrinolytic system,     Acta Chem. Scand., 24: 569-579, 1970.
10. Frisch, E. P., et al, Dosage of i. v. brinase in man based on brinase inhibitor capacity and coagulation studies, Angiology, 26:557, 1975.
11. Roschlau, H. E. and Fisher, A.M., Thrombolytic therapy with local perfusions of CA-7 (fibrinolytic enzyme from Aspergillus oryzae) in the dog,     Angiology, 17:670-682, 1966.
12. Larson, L. J., et al Properties of the complex between alpha-2-macro-globulin and brinase, a proteinase from Aspergillus oryzae with     thrombolytic effect, thrombosis Research, 49:55-68, 1988.
13. Verhaege, R, et al, Clinical trial of brinase and anticoagulants as a method of treatment for advanced limb ischemia, Eur. J. Clin. Pharmacol., 16: 165- 170, 1979.
14. Vanhove, P., et al, Action of brinase on human fibrinogen and plasminogen. Thrombos Haemostas., 42: 571-581, 1979
15. Frisch, E. P. and Blomback, M., Blood coagulation studies in patients treated with brinase. In: Progress in Chemical Fibrinolysis and     Thrombolysis. Vol. IV, J. F. Davidson (Ed.), Edinburgh: Churchill-Livingstone, pp. 184- 187, 1979
16. Phelan, J. J., et al, Coeliac disease: The abolition of gliadin toxicity by enzymes from Aspergillus niger, Clin. Sci. Molec. Med., 53:                    35-43,1977.
17. McCarthy, C. F., Nutritional defects in patients with malabsorption, Proc. Nutr. Soc., 35:37- 40,1976.
18. Gardner, M. L. G., Gastrointestinal absorption of intact proteins, Ann. Rev. Nutr., 8:329-350,1988.
19. Gardner, M. L. G., intestinal assimilation of intact peptides and proteins from the diet - A neglected field?, Biol. Rev., 59:289-331,1984.
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21. Udall, J. N. and Walker, W. A., The physiologic and pathologic basis for the transport of macromolecule's across the intestinal tract, J.                 Pediatr.. Gastroentarol. Nutr., :295-301,1982.
22. Loehry, C. A., et al Permeability of the small intestine to substances of different molecular weight, Gut, 11 :446-470, 1970.
23. Hemmings W. A. and Williams, E. W., Transport of large breakdown products of dietary protein through the gut wall Gut, 19:715-723, 1978.
24. Jacobson, I., et al Human beta-lactalbumin as a marker of rnacromolecular absorption, Gut, 27: 1029-1034, 1986.
25. Menzies, I. S., 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, 1984.
26. Wolf, J. L., et al Intestinal M cells: A pathway for entry of retrovirus into the host, Science, 212:471-472, 1981.
27. Ormistron B. J., 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 pp. 45-52, 1972.
28. Amoss, M., et al, Release of gonadotrophins by oral administration of synthetic LRF or a tripeptidle fragment of LRF, J. Clin. Endocrinol.              Metab., 35: 135-177, 1972.
29. Siefert, J., et al, Mucosal permeation of Macromolecules and particles, See Ref 31, pp. 505-513.
30. Laskowski M., et al, Effect of trypsin inhibitor on passage of insulin across the intestinal barrier, Science, 127: 1115-1116, 1958.
31. Liebow, C. and Rothman, S. S., Enteropancreatic circulation of digestive enzymes, Science, 189:472-474,1975
32. Bockman, D. E. and Winborm, W. B., Light and electron microscopy of intestinal ferritin absorption: Observations in sensitized and                     non-sensitized hamsters, Anat. Rec.,155:603- 622,1966.
33. Andre, C., et al Interference of oral immunization with the intestinal absorption of heterologous albumin, Eur. J. Immunol., 4:701-704, 1974.
34. Dannaeus A., et al, Intestinal uptake of ovalbumin in malabsorption and food allergy in relation to serum lgG antibody and orally administrated       sodium chromoglycate, Clin. Allergy, 9: 263-270,1979.
35. Ferguson, A. and Caldwell, F., Precipitins to dietary proteins in serum and upper GI secretion of coeliac children, Br. Med. J., 1 :75-77,1972.
36. Husby, S., et al Passage of dietary antigens into the blood of children with coeliac disease: Quantification and size distribution of absorbed       antigens, Gut, 28:1062-1072,1987.
37. Husby, S., et al 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,
      1986. 38. Walker, W. A., Antigen absorption from the small intestine and gastrointestinal disease, Pediatr. Clin., North Am., 22:731-746,              1975.
39. Hamilton, I., et al, Small intestinal permeability in dermatological disease, Q. J. Med., 56:559-567, 1985
40. Bjarnason, I., et al, Intestinal permeability in celiac sprue, dermatitis herpetiformis, schizophrenia and atopic eczema, Gastroenterology, 86:       1029, 1984.
41. Heatley, RV., et al, Inflammatory bowel disease, In Gut Defenses in Clinical Practice, M. S. Losowsky and R V. Heatley, eds., Churchill              Livingstone, Edinburgh, pp. 225-277, 1986.
42. Shorter, R G., et al, A working hypothesis for the etiology and pathogenesis of nonspecific inflammatory bowel disease, Am. J. Dig. Dis., 17:       1024-1032, 1972.
43. Jackson, P. G., et al, Intestinal permeability in patients with

You can expect a lot of documented research to come from the Nutritionist and owner of Optimal Health Systems (OHS), our new partner Doug Grant, in the upcoming Puzzle Pieces.  He has multiple patents in his (1) Whole Food, (2) All Predigested Natural Line.

Yours in Health and Wellness,
John W. Brimhall, BA, BS, DC, FIAMA, DIBAK

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