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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.
1. Griffin, S. M., et al,
Acid resistant lipase as replacement therapy in chronic exocrine
insufficiency: a study in dogs, Gut, 30:1012-1015, 1989.
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.
20. Warshaw, A. L., et a,
Protein uptake by the intestine: Evidence for absorption of intact
macromolecule's, Gastroenterology, 66: 987-992,1974.
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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