Posted on Saturday, 13th February 2010 by admin

enzymes

Virtually all living things – including those we cook and eat – contain enzymes. Enzymes, which act as the spark plugs for the vast majority of chemical reactions that make life possible, are a sine qua non for life.

Although most food eaten in the United States has been cooked, which inactivates the enzymes it contains, all the plant and animal foods in our meals are derived from once-living, enzyme-abundant things.

Over 2,500 different kinds of enzymes are found in living things. All enzymes are proteins, very special kinds of proteins that act as catalysts. Enzymes give our body chemistry its vitality, literally giving our metabolism a jump start. Plus, as molecules that enable the breaking down of our food, they also play a critically important role within our digestive system. Enzymes in our saliva allow us to break apart starches. Enzymes in our stomach help us break apart proteins. Enzymes in our intestines help us break apart fats, proteins, and carbohydrates of all kinds.

When we eat fresh, uncooked foods, those foods can still contain active enzymes. When we chew a freshly picked leaf of lettuce, we break the cells in the leaf apart, releasing its nutrients, including enzymes. Enzymes are not automatically destroyed by the acids or temperatures in our digestive tract. Enzymes in the stomach – called gastric enzymes – are specially designed to function in the stomach’s extremely acid conditions and are critical to our health. Our bodies can overheat from fever, extreme exercise or summer weather, but not to temperatures that will prevent the enzymes inside us from continuing to function.

Our digestive tract has specialized areas for absorbing large molecules, including enzymes (which are proteins), from food into our bloodstream. These areas house our M cells. M cells are specialized cells designed to selectively deliver large molecules from our intestines into our cells and bloodstream. The passing of enzymes from a mother to her nursing newborn is a good example of this M cell function. A mother’s milk contains the milk sugar, lactose. An enzyme called lactase is needed to digest lactose, but an infant’s body is not yet capable of manufacturing this enzyme. So, the mother sends lactase along with her milk, and in this way enables the baby to digest and absorb its lactose.

Ordinarily, we cook food at temperatures at least twice that of normal body temperature. For this reason, fresh, raw plant foods are our primary source of food enzymes. (Due to their high potential for bacterial contamination, most animal foods would be too risky for us to eat raw). While there have been no large scale, controlled studies to document the impact of enzyme-containing, fresh, raw plant foods on digestion and health, practitioners in fields of complementary, natural, and functional medicine have used enzyme supplementation successfully to help treat a wide variety of health problems and have long advocated the inclusion of fresh, organic, raw plant foods in the diet.

For serving size for specific foods, see Nutrient Rating Chart below at the bottom of this page.

  • Description
  • Function
  • Deficiency Symptoms
  • Toxicity Symptoms
  • Cooking, storage and processing
  • Factors that affect function
  • Drug-nutrient interaction
  • Nutrient interaction
  • Health conditions
  • Supplements
  • Food Sources
  • Public Recommendations
  • References

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.

Drug-Nutrient Interactions

Bromelain, the enzyme found in pineapple, seems to increase the absorption of antiobiotics, notably amoxicillin and tetracycline. In addition, since bromelain and papain (an enzyme found in papaya) act as blood thinners, it is suggested that they may increase the effect of warfarin, aspirin and other anticoagulant medications.

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:

  • Maldigestion and malabsorption
  • Pancreatic insufficiency
  • Steatorrhea (diarrhea due to fat malabsorption)
  • Celiac disease
  • Lactose intolerance
  • Thrombotic disease
  • Acute sinusitis
  • Post-operative recovery
  • Sports injuries
  • Adverse food reactions

Form in Dietary Supplements

As a supplement, dietary enzymes can be found either as individual compounds or in combination products that combine more than one type of enzyme. The combination products may either feature enzymes that are specific for one type of macronutrient (for example, a variety of proteases for protein digestion) or they may be a broad-spectrum product that features enzymes that catabolize carbohydrates, proteins and fats. Since protein-digesting enzymes can be denatured in the stomach, these supplements are oftentimes enteric coated, so they do not dissolve in the stomach but in the small intestine.

Some enzyme supplements are manufactured from animal sources while others are from non-animal sources. A popular, and effective, non-animal source of enzymes is Aspergillus oryzae, a type of fungus (Aspergillus is also used in the traditional Japanese technique of fermenting soybeans to produce soy sauce, tamari and miso). Bromelain and papain are two examples of enzymes derived from plants.

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.

 

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

  • Alternative Medicine Review. Monograph:Bromelain. Altern Med Rev. 1998 Aug;3(4):302-5. 1998. PMID:9727080.
  • 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.
  • Bland J and Berquist B. Nutrient content of germinated seeds. J John Bastyr Coll Naturop Med 1980: 2(1):3-9 1980.
  • 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.
  • 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.
  • Gardner, M. L. Gastrointestinal absorption of intact proteins. Annu Rev Nutr. 1988; 8:329-50 1988.
  • 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.
  • 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.
  • Gerbert G. Physiologie. Physiologie. Schattauer Publishing Co., Stuttgart, Gemany 1987.
  • Griffin SM. Acid resistant lipase as replacement therapy in chronic pancreatic exocrine insufficiency: a study in dogs. Gut 1989;30:1012-1015 1989.
  • Groff JL, Gropper SS, Hunt SM. Advanced Nutrition and Human Metabolism. West Publishing Company, New York, 1995 1995.
  • 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.
  • O’Keefe S. The use of lactase enzyme in feeding malnourished lactose intolerant patients. XIII International Congress of Nutrition, Brighton, England 1985: 190 1985.
  • Pizzorno J, Murray M. The Textbook of Natural Medicine. The Textbook of Natural Medicine 1998.
  • 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.
  • 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.
  • Trier, JS. Structure and function of intestinal M cells. Gastroenterol Clin North Am. 1991 Sep; 20(3):531-47 1991.

Comments (0)

Posted on Thursday, 11th February 2010 by admin

The two dipeptidyl-peptidase-4 inhibitors available in the U.S. are sitagliptin (sold as Januvia) and saxagliptin (sold as Onglyza). Vildagliptin is available in other countries.

Remember that drug names vary by country and manufacturer. This is a brief drug review; consult your physician or pharmacist for details.

How do they work?

DPP-4 inhibitors decrease both fasting and after-meal blood sugar levels primarily by increasing insulin release from pancreas beta cells. How they do it is complicated.

First off, you need to know that two gastrointestinal hormones levels—glucagon-like peptide-1 (GLP-1) and gastric inhibitory polypeptide—increase in response to a meal. These hormones increase insulin secretion by pancreas beta cells, suppress glucagon secretion from pancreas alpha cells after meals, help suppress glucose production by the liver, and improve glucose uptake by tissues outside the liver. GLP-1 also slows emptying by the stomach and reduces food intake. All this tends to lower glucose levels after meals.

Did I mention it was complicated?

If we could make these gut hormones hang around longer, their glucose-lowering action would be enhanced. How can we make them hang around and work longer? Easy: suppress the enzyme that degrades them: dipeptidyl-peptidase-4. That’s what DPP-4 inhibitors do.

The small intestine hormone GLP-1 is a major player in normal carbohydrate metabolism. GLP-1 levels, by the way, are decreased in type 2 diabetes.

For the DPP-4 inhibitors, we have no data on long-term safety, mortality, or diabetic complications.

Uses

Sitagliptin is FDA-approved as initial drug therapy for the treatment of type 2 diabetes, and as a second agent in those who do not respond to a single agent, such as metformin, a sulfonylurea, or a thiazolidinedione. It can also be used as a third agent when dual therapy with a sulfonylurea and metformin does not provide adequate blood sugar control.

Saxagliptin is FDA-approved as initial drug therapy for the treatment of type 2 diabetes or as an add-on drug for those who do not respond to a single drug, such as metformin, a sulfonylurea, or a thiazolidinedione.

Dosing

The DPP-4 inhibitors are given by mouth. The usual dose of sitagliptin is 100 mg once daily, with reduction to 50 mg for moderate to severe kidney impairment and 25 mg for severe kidney impairment. The usual dose of saxagliptin is 2.5 or 5 mg once daily, with the 2.5 mg dose recommended for patients with moderate to severe kidney impairment.

Side Effects

Generally well-tolerated. No risk of hypoglycemia when used as the sole diabetes drug. They do not cause weight gain. Sitagliptin might cause pancreatitis.

Comments (0)

Posted on Wednesday, 10th February 2010 by admin

You can hear all the rave about MonaVie products on T.V., websites, and from everyday people. If you are trying to decide if MonaVie is right for you, you can review the product or the distributor reviews. You can view both to get the best idea of how the MonaVie products can benefit you. Do not be afraid to utilize the experience of distributers.

It is easy to search for MonaVie products through your favorite search engine. You will find all you need on MonaVie to make an informed decision about whether or not it is right for you. You can start by looking into nutrition sites. Results are very high on search engines, since MonaVie has caught on so fast.

You will never get a 100% positive opinion on any product. The reviews have been very positive up to this point. As far as the independent distributor opinions go, that tends to vary. When trying to read reviews make sure that you are looking at why people are happy or unhappy.

Not everyone in the world is going to like MonaVie. We all have individual tastes. Being a distributor is not for everyone. Go with the majority of reviews. If you are finding more good reviews than bad, you are probably making a good decision either buying MonaVie as a product, or joining the MonaVie team as a distributor. So far, the majority loves Mona Vie.

When you are participating in your search for reviews, make sure to look at MonaVie related sites along with sites that have research studies on the subject of MonaVie. Sometimes they can give a different angle on what the product is all about. Taste will not often outweigh scientific evidence that a product works. It also doesn’t hurt to check with independent distributors. They use the products themselves, and can explain the benefits of how the product works within the body.

The best way to make a decision on MonaVie is to try it yourself. You will be trying a product with some of the highest quality ingredients on the market today. Some people who are very healthy may not feel the benefits of MonaVie. It does continue to work on the cellular level where you will get the most benefit; you will just not feel it working. It will help maintain your good health and fight against illness.

Read what people are saying about MonaVie on our Facebook fan page!

Tags: ,
Comments (0)

Posted on Wednesday, 10th February 2010 by admin

GLP-1 analogues available in the U.S. are exenatide (sold as Byetta) and liraglutide (sold as Victoza). They are sometimes referred to as GLP-1 receptor agonists. They are not considered first-choice drugs, but instead are typically used in combination with other drugs (except insulin).

Remember that drug names vary by country and manufacturer. This is a brief review only; consult your physician or pharmacist for full details.

Fun Fact for the diabetic version of Trivial Pursuit:

Exenatide (Byetta) is a synthesized version of a protein initially discovered in the saliva of a lizard, the Gila monster.

How do they work?

It’s complicated.

First off, you need to know that a small intestine hormone, glucagon-like peptide-1 (GLP-1), is produced in response to a meal. This hormone increases insulin secretion by pancreas beta cells, suppresses glucagon after meals, inhibits emptying of the stomach, and inhibits appetite. Other effects are suppression of glucose production by the liver, and improved glucose uptake by tissues outside the liver. All this tends to lower blood sugar levels after meals.

The problem is that GLP-1 is quickly destroyed by an enzyme called DPP-4. We have available to us now chemicals similar to GLP-1, called GLP-1 analogues, that bind to the GLP-1 receptors and are resistant to degradation by the enzyme DPP-4. They essentially act like GLP-1, and they hang around longer.

GLP-1 levels, by the way, are decreased in type 2 diabetes.

The action of GLP-1 is dependent on blood sugar levels. If blood glucose is not elevated, GLP-1 doesn’t go to work. From a practical viewpoint, this means that GLP-1-based therapies don’t cause hypoglycemia.

We know little about long-term outcomes with these drugs, such as diabetic complications, health-related quality of life, or mortality.

Uses

Exenatide is FDA-approved for adults with type 2 diabetes who are not adequately controlled with metformin, sulfonylurea, or a thiazolidinedione (or a combination of these agents). So it’s an add-on drug, not approved for use by itself. It’s not approved for use with insulin therapy.

Liraglutide is FDA-approved for treatment of type 2 diabetes but is not recommended as initial therapy, although it does seem to be approved for use by itself. It has been used alone and also in combination with metformin, sulfonylurea, and/or thiazolidinediones. It’s not approved for use with insulin therapy.

Dosing

They are available only as subcutaneous injections. Exenatide is twice daily, starting at 5 mcg within 60 minutes prior to a meal. After four weeks, the dose is increased to 10 mcg wtice daily.

Liraglutide is a once daily subcutaneous injection starting at 0.6 mg, increasing to 1.2 mg after one week. It is given without regard to meals. Maximum dose is 1.8 mg/day.

Side Effects

GLP-1 analogues tend to cause nausea, vomiting, and diarrhea in as many as four in 10 users. The nausea typically improves over time. They tend to cause weight loss. Both drugs might cause pancreatitis, which is life-threatening. When used with a sulfonlyurea, hypoglycemia may occur.

Liraglutide might cause thyroid cancer. No risk of hypoglycemia when used as the sole diabetes drug.

Comments (0)