Digestive Enzymes

Enzymes are protein molecules that carry a vital energy factor needed for every chemical action and reaction that occurs in our bodies. There are approximately 2,700 different enzymes found in the human body. These enzymes can combine with co-enzymes to form nearly one hundred thousand various chemicals that help us to see, hear, feel, move, digest food, and think. Every organ, every tissue, and all the one hundred trillion cells in our body depend upon the reaction of enzymes and their energy factor. Nutrition cannot be explained without describing the vital role played by enzymes. - Protease refers to a group of enzymes whose catalytic function is to hydrolyze (breakdown) peptide bonds of proteins. They are also called proteolytic enzymes or proteinases. Proteases vary in the susceptibility of the peptide bonds that they hydrolyze. Examples of proteases include: fungal protease, pepsin, trypsin, chymotrypsin, papain, bromelain, subtilisin, etc ... Proteolytic enzymes are very important in digestion as they breakdown the protein foods to liberate the amino acids needed by the body. Additionally, proteolytic enzymes have been used for centuries various forms of therapy. Their use in medicine is gaining more and more attention as several clinical studies are indicating their benefits in oncology, inflammatory conditions, blood theology, and immune regulation.

Contrary to old beliefs, several studies have shown that orally ingested enzymes can by-pass the conditions of the GI tract and be absorbed into the blood stream while still maintaining their enzymatic activity. While in the blood, proteinases are taken up by alpha-macroglobulin and other antiproteinases. However, the binding of alpha-macroglobulin to proteinases does not inactivate the enzyme, but rather ensure its clearance from the circulation after it has performed its enzymatic activity. As in the cases of lipases and amylases, proteases are also commercially produced in highly controlled aseptic conditions food supplementation and systemic enzyme therapy. The organisms most often used are Aspergillus niger and oryzae.

Oxidative reactions generate free radical damages to various molecules including proteins. Free radicals have been implicated in accelerating the aging process as well as several diseases, including diabetes, atherosclerosis, and neurodegenerative conditions. Under proper conditions of nutrition and adequate activity of antioxidant enzymes, the body handles and corrects the free radical damages. However, in many instances, the body is overwhelmed by the load of pro-oxidants (free radical generating molecules), resulting in oxidative stress conditions. One consequence of oxidative stress is the formation of oxidized proteins. Oxidized proteins often loose their function (become inactive), and undergo unfolding or conformational change of their structure which enhances their susceptibility to proteinases.

For instance, oxidized proteins in blood or extracellular fluid, include hormones, immune system proteins, transport proteins, and other proteins needed at various cellular locations. As these oxidized proteins loose their biological function, they may not carry out the cellular tasks and biochemical reactions they are meant to perform. For instance, an oxidized hormone may not be able to attach to its receptor on the cell surface; an oxidized enzyme may not perform its activity; an oxidized antibody molecule will not bind adequately to its antigen. Oxidative reactions occur in chains and in a cascade manner. Therefore, oxidation of one protein may lead to further oxidation reactions within the same molecule and/or other molecules which amplify the damaging effect. Thus, any oxidation of a protein if not corrected may result in impairment of biochemical functions of vital importance to the cellular viability. In order to avoid the cascade effect, oxidized proteins may be removed by an antioxidant enzyme or vitamin, or by proteolysis.

Oral proteases taken on an empty stomach have been shown to be absorbed and carried into the blood stream where they are bound to a2-macroglobulin.The binding of the a2-macroglobulin to proteases does not inactivate the proteolytic activity of the protease. However, the complexing of the a2-macroglobulin ensures the clearance of the protease from the organism. Several studies have indicated that oral proteases bound to the macroglobulins hydrolyze immune complexes, proteinaceous debris, damaged proteins, and acute phase plasma proteins in the blood stream. It is suggested that oral proteases may help hydrlyze and remove extracelluar proteins damaged by free radicals. This is based on the absorbability of the protease into the circulatory system, their hydrolytic activity and ability to remove proteinaceous debris in blood and extracellular fluid, and their susceptibility due to their unfolding and other conformational modifications from their native state. And oral fungal heavy metals such as lead (Pb) and mercury (Hg), exert their poisoning effect by binding to ionizable or sulfhydryl groups of proteins, including vital enzymes. Once they bind to an essential functional protein, such as an enzyme, they denature and/or inhibit it. This interaction of heavy metals to proteins can lead to degenerating diseases, nerve damage or even death. It should be noted that protease when taken on an empty stomach is readily taken up into the mucosa cells of the intestine and passed into the blood circulation. Clinical observations have noted that upon high intake of oral protease, heavy metal concentrations have been significantly decreased in the blood. This may be due to the binding of these toxic substances with the supplemental protease enzymes, as in the use of raw egg or milk in cases of accidental mercury ingestion. This binding facilitates the removal of toxic substances, thus avoiding a life-threatening situation of poisoning. Following that same concept, the addition of a strong, wide range pH protease can spare other vital proteins from heavy metal poisoning. - Amylase is an enzyme that hydrolyzes starch to disaccharide maltose and dextrins. The maltose is further broken down by maltase into glucose. The dextrins are further broken down by amylase and glucoamylase. Amylase specifically hydrolyzes the alpha-glucosidic linkages in starch and similar carbohydrates. Amylase is produced by the salivary glands, the pancreas, and also by some microorganisms. Aspergillus oryzae and niger have been used in the production of commercial amylases for food supplementation. - Lipase is an enzyme that hydrolyzes the ester bonds in mono, di, and triglycerides to form fatty acids and glycerol. Although some lipase is found in the stomach, most of the digestive lipase in humans is produced by the pancreas and secreted into the duodenum where it hydrolyzes the ingested dietary fats that have been emulsified by the bile. Besides the digestive lipase in the GI tract, there is also a hormone sensitive lipase that serves to mobilize and hydrolyze lipids in adipose tissues for energy purposes in the body. This hormone sensitive lipase is under the influence of several hormones. For instance, insulin inhibits this lipase: when carbohydrates, i.e., glucose, is high such as after a meal, insulin inhibits the further release of fatty acids, thus enhancing lipogenesis, the formation of adipose tissue, as opposed to breaking down fats.

However, there are other hormones that enhance the activity of the lipase when the body needs more energy and the carbohydrate levels don't need the immediate energy needs. Such hormones that release free fatty acids in the plasma for tissues to use as energy sources are epinephrine, norepinephrine, glucagon, adrenocorticotropic hormone (ACTH), alpha and beta melanocyte stimulating hormones and growth hormone. As amylase, lipase is also produced on large scale by microorganisms including Aspergillus oryzae. This fungus produces a very potent lipase that is used in food supplementation. Lipase in food digestion is very important to ensure breakdown of fats, and adequate supply of fat soluble vitamins. It should be noted that all cell membranes and other structures are made up of lipids: thus, an adequate supply of essential fatty acids in the diet are important to ensure viable cells.

- Cellulase enzymes digest cellulose fiber and breaks it down to beta-glucose (blood sugar). The wall of the Candida yeast cell is composed largely of chitin a cellulose like fiber, and it is vulnerable to digestion by Cellulase enzymes. This is great news for people afflicted with Candida. - Glucoamylase removes the D-glucose residues by hydrolyzing the alpha-glucosodic bonds. A particular isoform of glucoamylase in Aspergillus niger has been shown to hydrolyze the alpha-glucosidic bonds of the branching chains found in amylopectin. - Sucrose (what we know as household sugar) is actually two sugars joined together. The proper term for this is a disaccharide. Sucrose consists of a glucose and fructose molecule joined together. Invertase splits the bond between the two sugars by hydrolysis to make them available to the body as a nutrient for energy production. - Catalase is a common enzyme found in nearly all living organisms which are exposed to oxygen. Catalase has one of the highest turnover numbers of all enzymes; one molecule of catalase can convert millions of molecules of hydrogen peroxide to water and oxygen per second. The function of the enzyme catalase is to break down the chemical hydrogen peroxide inside living cells. Because it is toxic, or poisonous, hydrogen peroxide would soon kill the cell if it were not removed or broken down immediately. - AGS a-Galactosidase is an enzyme derived from the fungus Aspergillus niger. It hydrolyzes the non-reducing galactocide residues from poly and oligosaccharides in an exo-fashion. These poly-saccharides (primarily raffinose, stacchiose, and melibiosc) are typically found in legumes and are not digestible in the small intestine. If these sugars are not absorbed, they pass into the large intestine. In the large intestine, these sugars are fermented by native microbial flora and produce gas resulting in bloating, pain and general discomfort. - Beta Glucanase is a very important enzyme because the human body cannot produce it on its own. Beta Glucanase helps in the breakdown of plant walls (cellulose), and increases the overall efficiency of binding excess cholesterol and toxins in the intestines for removal. Beta Glucanase may be beneficial for food and environmental allergies, drug withdrawal, cell detox, colon cleaning and pain syndromes, Candida(yeast infections), gas, bloating, acute food allergies, facial pain or paralysis. Beta-glucanase is particularly effective in breaking down glucan, a type of carbohydrate that is found in wheat and barley which is very beneficial for people who are unable to digest grains. - Pactinase breaks down pectin, a non-cellulose polysaccharide commonly found in fruits and vegetables. - Xylanase Hydrolyzes plant polysaccharides (long-chain carbohydrates), particularly non-starch polysaccharides (NSP's). Non-starch polysaccharides include the arabinoxylans. Although arabinoxylans are most typically associated with wheat and wheat by-products. Soluble arabinoxylans can increase the viscosity, or gel-formation, of the intestinal contents therefore impairing nutrient uptake. Insoluble arabinoxylans within plant cell walls contain nutrients such as starch and protein. This allows valuable nutrients to by-pass digestion if not not broken down. - Phytase is an enzyme that can break down the undigestible phytic acid (phytate) part found in grains and oil seeds and thus release digestible phosphorus, calcium and other nutrients. Humans do not produce this enzyme naturally. Supplementing with phytase, makes available bound nutrients like calcium, phosphorus, other minerals, carbohydrates and proteins. - Hemicellulase is a group of enzymes that hydrolyzes the complex polysaccharides known as hemicellulose. Hemicellulose is highly viscous (sticky) compounds that bind digestive enzymes and decrease the rate of nutrient assimilation. Hemicellulase increases protein absorption from various grains. - Lactase is essential for digestive hydrolysis of lactose in milk. Deficiency of the enzyme causes lactose intolerance. Lactose intolerance is an inability to digest and absorb lactose (the sugar in milk) that results in gastrointestinal symptoms when milk or products containing milk are drunk or eaten. Lactose is a larger sugar that is made up of two smaller sugars, glucose and galactose. In order for lactose to be absorbed from the intestine and into the body, it must first be split into glucose and galactose. The glucose and galactose then are absorbed by the cells lining the small intestine. The enzyme that splits lactose into glucose and galactose is called lactase, and it is located on the surface of the cells that line the small intestine. - Bromelain is a mixture of enzymes found naturally in the juice and stems of pineapples. Called a proteolytic enzyme, bromelain is believed to help with the digestion of protein. There is some evidence that bromelain supplements may reduce swelling, bruising, inflammation and pain after surgery and injury. In Germany, bromelain has been approved for these uses by the Commission E since 1993. - The enzyme papain is extracted when the papaya is still unripe, and can be put into capsule or chewable form as a digestive aid. It is a proteolytic enzyme that work to break down complex proteins to produce small peptides and amino acids that can be better utilized or transported to other parts of the body.