enzymes

Foods Richest in enzymes

No food chart data available.

About enzymes

Description

Enzymes are not difficult to pick out in a science book, because 90% of all enzymes are given scientific names that end in the letters -ase. Following are two types of enzymes contained in foods.

Digestive Enzymes

Plant foods contain many of the same enzymes that humans use to metabolize different kinds of macronutrients. Proteases and peptidases, which help digest protein; lipases, which help digest fat; and cellulases and saccharidases, which help digest starches and sugars are examples of the kind of digestive enzymes that would normally secreted in our digestive tract or in a nearby organs like the pancreas or liver. However, these same digestive enzymes can be found in the plant foods that we eat.

Antioxidant Enzymes

Like humans, plants must protect themselves against oxygen-related damage, and they depend on enzymes to help them do so. A recently germinated sprout, for example, starts to generate many new oxidative enzymes in preparation for its journey up through the soil and into the open air. Superoxide dismutase (SOD) and catalase (CAT) are examples of oxidative enzymes that occur in higher concentrations in young plant sprouts than in the older, mature leaves. Glutathione peroxidase (GPO) is another example of an important oxidative enzyme that is found in the human body and in the plants we eat.

How it Functions

Necessary for Proper Digestion

Digestive enzymes play an integral role in the digestion of proteins, fats and carbohydrates since they catabolize these macronutrients into smaller molecules, which can be absorbed in the intestines. Our optimal physiological functioning depends upon the proper digestion and absorption of these nutrients.

Confers Inflammatory and Oxidative Protection

Certain enzymes, such as bromelain (found in pineapple), have anti-inflammatory properties. Bromelain seems to confer anti-inflammatory protection through a variety of mechanisms. It is thought to inhibit intermediates of the clotting cascade, increase fibrinolysis (the dissolution of clots), and reduce the production of inflammatory molecules such as bradykinin.

Support for the Immune System

Enzymes support the immune system in a few different ways. Since enzymes can work on substrates wherever the substrate is found, some of their targets include molecules other than the macronutrients associated with food. For example, protease enzymes can break apart the proteins that are found in unwanted bacteria and therefore reduce our risk of infection. In addition, the enzyme bromelain has been found to increase the production of a host of different immune system messenger molecules, including cytokines such as tumor necrosis factor-alpha, interleukin-1-beta and interleukin-6.

Promoting General Metabolic Eficiency

Evidence shows that the body conserves it own digestive enzymes by absorbing intact both endogenous (produced in the body) and exogenous (supplemented to the body by food or supplement) enzymes. Exogenous pancreatic enzymes have been found to be absorbed intact from the gut, transported through the bloodstream, taken up by the pancreatic cells, and resecreted into the intenstines by the pancreas, mixed with newly synthesized pancreatic enzymes. It is suggested that oral supplementation of enzymes may have a sparing effect on the body’s own digestive enzymes, perhaps aiding organ regeneration, by breaking down substrates, such as foods, for which endogenous enzymes would otherwise be used, thus freeing these enzymes for other beneficial activities.

Deficiency Symptoms

There is no research on symptoms of food enzyme deficiency. The clinical experience of many health care practitioners suggests that symptoms related to dyspepsia (indigestion), including heartburn, flatulence, belching and the appearance of undigested food in stool, may suggest enzyme deficiency since these symptoms could be caused by the improper digestion of food, which would occur with a deficiency of digestive enzymes.

Toxicity Symptoms

There is no research on food enzyme toxicity. Enzymes in supplement form may cause allergenic reactions due to the introduction of novel proteins which may increase the risk of antigenic reaction, particularly in immune-compromised individuals. In addition, bromelain may cause allergenic reactions as it has been shown to promote certain types of antibody mediated reactions.

Impact of Cooking, Storage and Processing

Cooking foods at virtually all standard cooking temperatures denatures enzymes, destroying their functioning.

The majority of processing techniques used by food manufacturers destroys the natural enzymes found in foods.

The effects of storage on enzyme integrity varies greatly, depending upon temperature and duration. The higher the temperature and the longer the food is stored, the greater likelihood that any enzymes it contains will be denatured.

Factors that Affect Function

Different enzymes have optimal pH ranges at which the reaction that they catalyze will occur most rapidly.

Temperature can affect enzyme activity level. Increased temperatures increase the rate at which an enzyme will catalyze a reaction, yet only up to a point, since too high a temperature will cause the enzyme to denature, destroying its activity.

Certain heavy metals inhibit the activity of enzymes by interrupting the reactions in which they are involved. These heavy metals include barium, lead and mercury.

Nutrient Interactions

There is limited research on the interaction between enzymes and nutrients, although some minerals serve as cofactors for certain endogenously produced enzymes. Studies have suggested that pancreatin supplementation may reduce folic acid absorption.

Health Conditions

A high dietary intake of enzymes may play a role in the prevention and/or treatment of the following health conditions:

Food Sources

Virtually all fresh, organically grown, uncooked plant foods are sources of enzymes. Bromelain is found in pineapples while papain is concentrated in unripe papayas.

Nutrient Rating Chart

Food Source Analysis not Available for this Nutrient

Public Health Recommendations

No public health recommendations for dietary intake of enzymes have been made by any established health agency or organization.

References

  1. Alternative Medicine Review. Monograph:Bromelain. Altern Med Rev. 1998 Aug;3(4):302-5. 1998. PMID:9727080.
  2. Barillas C and Solomons NW. Effective reduction of lactose maldigestion by direct addition of beta-galactosidases to milk at mealtime. Pediatr 79:766-772. 1987.
  3. Bland J and Berquist B. Nutrient content of germinated seeds. J John Bastyr Coll Naturop Med 1980: 2(1):3-9. 1980.
  4. Carroccio, A., Guarino, A., Zuin, G., Verghi, F., Berni Canani, R., Fontana, M. et al. Efficacy of oral pancreatic enzyme therapy for the treatment of fat malabsorption in HIV-infected patients. Aliment Pharmacol Ther. 2001 Oct; 15(10):1619-25. 2001.
  5. Gailhofer G, Wilders-Truschnig M, Smolle J, Ludvan M. Asthma caused by bromelain: an occupational allergy. Clin Allergy 1988 Sep;18(5):445-50. 1988. PMID:3233722.
  6. Gardner, M. L. Gastrointestinal absorption of intact proteins. Annu Rev Nutr. 1988; 8:329-50. 1988.
  7. Gardner, M. L.; Illingworth, K. M.; Kelleher, J., and Wood, D. Intestinal absorption of the intact peptide carnosine in man, and comparison with intestinal permeability to lactulose. J Physiol. 1991 Aug; 439:411-22. 1991.
  8. Gaspani L, Limiroli E, Ferrario P et al. In vivo and in vitro effects of bromelain on PGE(2) and SP concentrations in the inflammatory exudate in rats. Pharmacology 2002 May;65(2):83-6. 2002.
  9. Gerbert G. Physiologie. Physiologie. Schattauer Publishing Co., Stuttgart, Gemany. 1987.
  10. Griffin SM. Acid resistant lipase as replacement therapy in chronic pancreatic exocrine insufficiency: a study in dogs. Gut 1989;30:1012-1015. 1989.
  11. Groff JL, Gropper SS, Hunt SM. Advanced Nutrition and Human Metabolism. West Publishing Company, New York, 1995. 1995.
  12. Kerneis, S. and Pringault, E. Plasticity of the gastrointestinal epithelium: the M cell paradigm and opportunism of pathogenic microorganisms. Semin Immunol. 1999 Jun; 11(3):205-15. 1999.
  13. O'Keefe S. The use of lactase enzyme in feeding malnourished lactose intolerant patients. XIII International Congress of Nutrition, Brighton, England 1985: 190. 1985.
  14. Pizzorno J, Murray M. The Textbook of Natural Medicine. The Textbook of Natural Medicine. 1998.
  15. Russell RM, Dutta SK, Oaks EV, Rosenberg IH, Giovetti AC. Impairment of folic acid absorption by oral pancreatic extracts. Dig Dis Sci 1980 May;25(5):369-73. 1980.
  16. Shaw D, Leon C, Kolev S, et al. Traditional remedies and food supplements. A 5-year toxicological study (1991-1995). Drug Saf. 1997;17:342�356. 1997.
  17. Trier, JS. Structure and function of intestinal M cells. Gastroenterol Clin North Am. 1991 Sep; 20(3):531-47. 1991.
  18. Barillas C and Solomons NW. Effective reduction of lactose maldigestion by direct addition of beta-galactosidases to milk at mealtime. Pediatr 79:766-772 1987.
  19. Bland J and Berquist B. Nutrient content of germinated seeds. J John Bastyr Coll Naturop Med 1980: 2(1):3-9 1980.
  20. Gailhofer G, Wilders-Truschnig M, Smolle J, Ludvan M. Asthma caused by bromelain: an occupational allergy. Clin Allergy 1988 Sep;18(5):445-50 1988. PMID:3233722.
  21. Gardner, M. L. Gastrointestinal absorption of intact proteins. Annu Rev Nutr. 1988; 8:329-50 1988.
  22. Gardner, M. L.; Illingworth, K. M.; Kelleher, J., and Wood, D. Intestinal absorption of the intact peptide carnosine in man, and comparison with intestinal permeability to lactulose. J Physiol. 1991 Aug; 439:411-22 1991.
  23. Gaspani L, Limiroli E, Ferrario P et al. In vivo and in vitro effects of bromelain on PGE(2) and SP concentrations in the inflammatory exudate in rats. Pharmacology 2002 May;65(2):83-6 2002.
  24. Gerbert G. Physiologie. Physiologie. Schattauer Publishing Co., Stuttgart, Gemany 1987.
  25. Griffin SM. Acid resistant lipase as replacement therapy in chronic pancreatic exocrine insufficiency: a study in dogs. Gut 1989;30:1012-1015 1989.
  26. Groff JL, Gropper SS, Hunt SM. Advanced Nutrition and Human Metabolism. West Publishing Company, New York, 1995 1995.
  27. Kerneis, S. and Pringault, E. Plasticity of the gastrointestinal epithelium: the M cell paradigm and opportunism of pathogenic microorganisms. Semin Immunol. 1999 Jun; 11(3):205-15 1999.
  28. O'Keefe S. The use of lactase enzyme in feeding malnourished lactose intolerant patients. XIII International Congress of Nutrition, Brighton, England 1985: 190 1985.
  29. Pizzorno J, Murray M. The Textbook of Natural Medicine. The Textbook of Natural Medicine 1998.
  30. Russell RM, Dutta SK, Oaks EV, Rosenberg IH, Giovetti AC. Impairment of folic acid absorption by oral pancreatic extracts. Dig Dis Sci 1980 May;25(5):369-73 1980.
  31. Shaw D, Leon C, Kolev S, et al. Traditional remedies and food supplements. A 5-year toxicological study (1991-1995). Drug Saf. 1997;17:342-356. 1997.
  32. Trier, JS. Structure and function of intestinal M cells. Gastroenterol Clin North Am. 1991 Sep; 20(3):531-47 1991.