DIGESTIVE ENZYME RESEARCH

 

Br J Nutr. 2002 May;87 Suppl 2:S145-51.

Gastrointestinal effects of prebiotics.

Cummings JH, Macfarlane GT.

Department of Molecular and Cellular Pathology,
University of Dundee, Ninewells Hospital and Medical School, UK. j.h.cummings@dundee.ac.uk

The defining effect of prebiotics is to stimulate selectively the growth of bifidobacteria and lactobacilli in the gut and, thereby, increase the body's natural resistance to invading pathogens. Prebiotic carbohydrates may also have additional, less specific, benefits because they are fermented in the large intestine. The prebiotic carbohydrates that have been evaluated in humans at the present time largely consist of fructans or galactans. There is consistent evidence from in vitro and in vivo studies that these are not digested by normal human enzymes, but are readily fermented by anaerobic bacteria in the large intestine. There are no reports of faecal recovery of measurable quantities of prebiotic carbohydrates. Through fermentation in the large intestine, prebiotic carbohydrates yield short-chain fatty acids, stimulate the growth of many bacterial species in addition to the selective effects on lactobacilli and bifidobacteria, they can also produce gas. Along with other fermented carbohydrates, prebiotics have mild laxative effects, although this has proved difficult to demonstrate in human studies because the magnitude of laxation is small. Potentially, the most important effect of prebiotic carbohydrates is to strengthen the body's resistance to invading pathogens and, thereby, prevent episodes of diarrhoea. At the present time, this effect has not been convincingly demonstrated in either adults or children, although there have been attempts to ameliorate the diarrhoea associated with antibiotics and travel, but without success. However, prebiotic carbohydrates clearly have significant and distinctive physiological effects in the human large intestine, and on the basis of this it is likely that they will ultimately be shown to be beneficial to health.


 

 

 

Am J Physiol Endocrinol Metab. 2004 Jan;286(1):E64-76. Epub 2003 Sep 9.

 



Branched-chain amino acid catabolism: unique segregation of pathway enzymes in organ systems and peripheral nerves.

Sweatt AJ, Wood M, Suryawan A, Wallin R, Willingham MC, Hutson SM.

Department of Biochemistry, Wake Forest University School of Medicine, Medical Center Boulevard, Winston-Salem, NC 27157, USA. asweatt@wfubmc.edu

We have examined the localization of the first two enzymes in the branched-chain amino acid (BCAA) catabolic pathway: the branched-chain aminotransferase (BCAT) isozymes (mitochondrial BCATm and cytosolic BCATc) and the branched-chain alpha-keto acid dehydrogenase (BCKD) enzyme complex. Antibodies specific for BCATm or BCATc were used to immunolocalize the respective isozymes in cryosections of rat tissues. BCATm was expressed in secretory epithelia throughout the digestive tract, with the most intense expression in the stomach. BCATm was also strongly expressed in secretory cells of the exocrine pancreas, uterus, and testis, as well as in the transporting epithelium of convoluted tubules in kidney. In muscle, BCATm was located in myofibrils. Liver, as predicted, was not immunoreactive for BCATm. Unexpectedly, BCATc was localized in elements of the autonomic innervation of the digestive tract, as well as in axons in the sciatic nerve. The distributions of BCATc and BCATm did not overlap. BCATm-expressing cells also expressed the second enzyme of the BCAA catabolic pathway, BCKD. In selected monkey and human tissues examined by immunoblot and/or immunohistochemistry, BCATm and BCATc were distributed in patterns very similar to those found in the rat. The results show that BCATm is in a position to regulate BCAA availability as protein precursors and anabolic signals in secretory portions of the digestive and other organ systems. The unique expression of BCATc in neurons of the peripheral nervous system, without coexpression of BCKD, raises new questions about the physiological function of this BCAT isozyme.

Enzyme Research

Research found thirty times more enzymes in the saliva of young adults than in that of persons sixty-nine years of age.
Howell, E. Enzyme Nutrition. Avery Publishing Co. 1985

Researchers have also found higher levels of amylase in the urine of young adults as compared to older adults.
Ivy, A., Schmidt, C., Beazell, J.. Journal of Nutrition. 12:59-83. 1936

Bartos and Groh enlisted ten young men and ten older men for a study in which they used a drug to stimulate the pancreatic juice flow. The juice was then pumped out and tested. The researchers discovered that considerably less of the enzyme amylase was present in the pancreatic juices of the older men.
Bartos and Groh. Proceedings of the Society for Experimental Biology and Medicine 37:613-615.

Other research indicates that not only are there fewer enzymes in the pancreas. But also in the trillions of cells in our bodies as we age.
Ivy, A., Schmidt, C., Beazell, J.. Journal of Nutrition. 12:59-83. 1936

Research on rats given supplemental enzymes showed that the supplemented rats had more enzymes than the control group of rats, clearly indicating the existence of a fixed enzyme potential. The enzyme-fed rats lived three years in comparison to two years for those rats fed an enzyme-free diet.
Howell, Edward. Food Enzymes for Health and Longevity. Lotus Press, 1994.

Research done on rats and chickens that were fed cooked foods revealed that the pancreas gland enlarged to handle the extra burden of the enzyme-deficient diet. Hence, the animals got sick and failed to grow. The pancreas is responsible for making and secreting many digestive enzymes. Our pancreas will enlarge when called upon to process more enzymes or digest cooked food. Ruminant animals such as cattle, goats, deer and sheep get along with pancreas about a third as large as ours because of their raw food diet. However, when these animals are fed heat-processed, enzyme-free food, their pancreas enlarged up to three times the normal size than when fed on a raw plant diet.
Grossman, M. Greengard, H, Ivy, A. American Journal of Physiology. 141:38-41, 1944


The following information is excerpted from a Transformation Enzyme Corporation white paper titled "Oral Enzymes: Facts and Concepts" by Dr. Mahamane Mamadou, Ph.D.

Effect of Oral Enzymes on the Immune System
Another molecule that directly impacts in the modulation of the immune system is alpha 2-macro-globulin. High concentrations of free alpha 2-macroglobulin in the blood hinders the activity of the immune system (Hubbard et al., 1987). However, when oral enzymes are taken and absorbed into the blood stream, they bind to the alpha 2-Macroglobulin, and thus reduce the concentrations of free alpha 2-macroglobulin. This reduction of alpha 2-macroglobulin has been shown to boost the immune system. Oral proteases and amylases have also been reported to modulate the secretion of cytokines (Desser et al., 1993). Cytokines are important immune messenger molecules that control the effectors immune cells. Additionally, oral enzymes help modulate and control cell adhesion molecules, receptors and other messenger molecules that tend to inhibit the immune system and/or provide anchor to metastatic cancer cells (Targoni et al., 1999).

  • Desser, L., Rehberger, A., et al. 1993: Cytokine production in human peripheral blood mono-nuclear cells after oral administration of the polyenzyme preparation Wobenzyme. Int. J. of Cancer Res. and Treatment 50:403.
  • Targoni, O.S., Tary-Lehmann, M., and Lehmann, P.V., 1999: Prevention of murine EAE by oral hydrolytic enzyme treatment. Journal of Autoimmunity 12:191.

Effect of Oral Enzymes on Other Human Health Conditions
The application of enzymes in clinical studies has encompassed various disease conditions, and the results have proven to be better therapeutic agents or at least equally effective as other conventional forms of treatments.

However, as enzymes have been shown to have fewer to absent side effects, their use may be a safer alternative. Some of the conditions where clinical enzyme studies were conducted include:

  • ovarian cancer (Lahousen, 1995);
  • herpes zoster (Kleine, 1993);
  • acute sinusitis (Rayn, 1967);
  • chronic pancreatitis (Isaakson, 1983);
  • chronic fatigue syndrome (Wilke, 1992; Ho-Yen, 1991);
  • prevent rejection of heart allograft (Gaciong et al., 1996); and
  • multiple myeloma (Sakalova, 1993);

This is just a brief list of areas where enzymes have been implicated as treatment agents. There are several other physiological, biochemical disorders as well as infectious diseases where enzymes have been proven to provide therapeutic benefits. The different roles of oral proteases are being continuously investigated in relation to various diseases and cancers, such as breast cancer, prostate cancer, AIDS, and other immune system disorders.

As indicated by the clinical data cited, the use of hydrolytic enzymes as therapeutic agents has been proven effective in many areas. Enzymes could be used alone or in combination with other medicinal agents to prevent and alleviate health disorders. Oral proteases perform most of their action as active adjuvants to "biological response modifiers" (BRM).

  • Lahousen, M. 1995: Wien med. Wschr. 145:663.
  • Kleine, M.W., 1993: A comparison between oral hydrolytic enzyme combination and oral acyclovir as therapy of acute zoster. J. Eur. Acad. Dermatol. Venereal. 2:296.
  • Rayn, R.E., 1967: A double-blind clinical evaluation of bromelain in the treatment of acute sinusitis. Headache 7:13.
  • Isaakson, J.I., and Ihse, I., 1983: Pain reduction by oral pancreatic enzyme preparation in chronic pancreatitis. Digest Dis. Sci. 28:97.
  • Wilke, W.S., 1992: Chronic fatigue and immune dysfunction. Cleveland Clin. J. Med. 59:123.
  • Ho-Yen, D.O., Billington, R.W., and Urquhart, J., 1991: Natural killer cells and the post viral fatigue syndrome. Scand. J. Infect. Dis. 23:711.
  • Gaciong, Z., Paczek, L., et al., 1996: Beneficial effect of proteases on allograft arteriosclerosis in a rat aortic model. Nephro. Dial. Transplant. 11:987.
  • Sakalova, A., Holomanova, D., et al., 1993: Prognostic value of plasma cell immunophenotype in patients with multiple myeloma. Neoplasma 40:351.