Wobenzym Ingredient and Uses

Ingredient Uses

Pancreatin

Pancreatin is a mixture of several digestive enzymes produced by the exocrine cells of the pancreas. It is composed of amylase, lipase and protease. This mixture is used to treat conditions in which pancreatic secretions are deficient, such as pancreatitis and cystic fibrosis. It has been claimed to help with food allergies, celiac disease, autoimmune disease, cancer, and weight loss. Pancreatin is sometimes called "pancreatic acid", although it is neither a single chemical substance nor an acid.

Pancreatin contains the pancreatic enzymes trypsin, amylase, and lipase. A similar mixture of enzymes is sold as pancrelipase, which contains more active lipase enzyme than does pancreatin. The trypsin found in pancreatin works to hydrolyze proteins to oligopetides; amylase hydrolyze starches to oligosaccharides and the disaccharide maltose; and lipase hydrolyzes triglycerides to fatty acids and glycerol's. Pancreatin is an effective enzyme supplement for replacing missing pancreatic enzymes, and aids in the digestion of foods in cases of pancreatic insufficiency.

Papain

Papain is a cysteine protease (EC 3.4.22.2) hydrolase enzyme present in papaya (Carica papaya) and mountain papaya (Vasconcellea cundinamarcensis). Its utility is in breaking down the tough meat fibers and has been utilized for thousands of years in its native South America. It is sold as a component in powdered meat tenderizer available in most supermarkets. Papain, in the form of a meat tenderizer such as Adolph's, made into a paste with water, is also a home remedy treatment for jellyfish, bee, yellow jacket (wasps) stings and possibly stingray wounds, breaking down the protein toxins in the venom. It is also the main ingredient in Stop Itch and Stop Itch Plus, a DermaTech Laboratories first aid cream popular in Australia.

Papain is used to dissociate cells in the first step of cell culture preparations. A 10 minute treatment of small tissue pieces (less than 1 mm cubed) will allow papain to begin breaking down the extracellular matrix molecules holding the cells together. After 10 minutes, the tissue should be treated with a protease inhibitor solution to stop the protease action (if left untreated papain's activity will lead to complete lysis of the cells). The tissue must then be triturated (passed quickly up and down through a Pasteur pipette) in order to break up the pieces of tissue into a single cell suspension.

It is also used as an ingredient in various enzymatic debriding preparations, notably Accuzyme. These are used in the care of some chronic wounds to clean up dead tissue.

It can also be found as an ingredient in some toothpastes or mints as teeth-whitener. Its whitening effect in toothpastes and mints however is minimal, because the papain is present in low concentrations, and will be quickly diluted by saliva. It would take several months of using the whitening product to have noticeably whiter teeth.

Bromelain

Bromelain can refer to one of two protease enzymes extracted from the plant family Bromeliaceae, or it can refer to a combination of those enzymes along with other compounds produced in an extract. Bromelain is a mixture of sulfur-containing protein-digesting enzymes called proteolytic enzymes or protease's and several other substances in smaller quantities. The two main enzymes are:

The other substances include peroxidase, acid phosphatase, protease inhibitors, and calcium.

Bromelain is present in all parts of the pineapple plant (Ananas comosus), but the stem is the most common commercial source, presumably because it is readily available after the fruit has been harvested. Pineapples have had a long tradition as a medicinal plant among the natives of South and Central America. However, just eating pineapple will not give you a great deal of extra bromelain, because it is mostly concentrated in the stem, which is not nearly as tasty (albeit still edible).

Bromelain can be used in a vast array of medical conditions. It was first introduced in this area in 1957, and works by blocking some proinflammatory metabolites that accelerate and worsen the inflammatory process. It is an anti-inflammatory agent, and so can be used for sports injury, trauma, arthritis, and other kinds of swelling. Its main uses are treatment of athletic injuries, digestive problems, phlebitis, sinusitis, and aiding healing after surgery.

It has also been proposed for the treatment of arthritis, chronic venous insufficiency, easy bruising, gout, hemorrhoids, menstrual pain, autoimmune disorders, ulcerative colitis, and sinusitis.

Studies have shown that bromelain can also be useful in the reduction of platelet clumping and blood clots in the bloodstream, especially in the arteries.

It may have treatment potential for HIV.

Proprietary bromelain mixtures are been used for third degree burn treatment, and more are being approved.

Its side effects include nausea, vomiting, diarrhea, menorrhagia (excessively heavy menstrual flow) and possible allergic reactions. One study has also associated Bromelain with increased heart rate.

Bromelain supplementation up to 460 mg has been shown to have no effect on human heart rate or blood pressure; however, increasing doses up to 1840 mg have been shown to increase the heart rate proportionately.

Trypsin

Trypsin (EC 3.4.21.4) is a serine protease found in the digestive system, where it breaks down proteins. Trypsin predominantly cleaves peptide chains at the carboxyl side of the amino acids lysine and arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation.

Trypsin is secreted into the duodenum, where it acts to hydrolyse proteins into smaller peptides or amino acids. This is necessary for the uptake of protein in the food. Trypsin catalyses the hydrolysis of peptide bonds. The enzymatic mechanism is like all other serine proteases: A catalytic triad serves to make the active site serine nucleophilic. This is achieved by modifying the electrostatic environment of the serine. The enzymatic reaction that trypsins catalyze is thermodynamically favorable but requires significant activation energy (it is "kinetically unfavorable"). Trypsins have an optimal operating pH of about 8 and optimal operating temperature of about 37°C.

The aspartate residue (Asp 189) located in the catalytic pocket (S1) of trypsins is responsible for attracting and stabilizing positively-charged lysine and/or arginine, and is thus responsible for the specificity of the enzyme. This means that trypsin predominantly cleaves proteins at the carboxyl side (or "C-terminal side") of the amino acids lysine and arginine, except when either is followed by proline. Trypsins are considered endopeptidases, i.e., the cleavage occurs within the polypeptide chain rather than at the terminal amino acids located at the ends of polypeptides.

Trypsin is produced in the pancreas in the form of inactive zymogen, trypsinogen. It is then secreted into the small intestine, where the enzyme enterokinase activates it into trypsin by proteolytic cleavage. The resulting trypsins themselves activate more trypsinogens (autocatalysis), so only a small amount of enterokinase is necessary to start the reaction. This activation mechanism is common for most serine proteases, and serves to prevent auto digestion of the pancreas.

The activity of trypsins is not affected by the inhibitor tosyl phenylalanyl chloromethyl ketone TPCK, which deactivates chymotrypsin. This is important because, in some applications, like mass spectrometry, the specificity of cleavage is important.

One consequence of inheriting the autosomal recessive disease cystic fibrosis is a deficiency of trypsin and other digestive enzymes from the pancreas. This leads to the disorder termed meconium ileus. This disorder involves intestinal obstruction (ileus) due to overly thick meconium which is normally broken down by trypsins and other proteases, then passed in feces.

Chymotrypsin

Chymotrypsin is a digestive enzyme that breaks down proteins (i.e., it is a proteolytic enzyme; it can also be referred to as a protease). It is naturally produced by the pancreas in the human body. However, it can also be taken as an enzyme supplement to improve health and digestion and aid in the treatment of various diseases.

The pancreas, which produces chymotrypsin and other digestive enzymes, is a digestive organ in the abdomen that is located just below the stomach. Its primary job is to produce enzymes required for the digestion and absorption of food. Each day the pancreas secrets about 1.5 qt (1.4 L) of pancreatic juice, consisting of enzymes, water, and electrolytes (primarily bicarbonate) into the small intestine. The enzymes are secreted in an inactive form (as proenzymes) so that they will not digest the pancreas. The pancreas secretes an inhibitor to ensure that the enzymes are not activated too early. When the pancreatic juice reaches the small intestine, the enzymes become activated. The small intestine is not digested because it contains a protective mucous lining. However, self-digestion can occur if the pancreatic duct becomes blocked or if the pancreas is damaged. The proenzymes can overwhelm the inhibitor, causing the enzymes to become active while in the pancreas. This condition, called acute pancreatitis, can result in a lifetime of pancreatic insufficiency.

The enzymes secreted by the pancreas break down food by breaking the chemical bonds that hold food molecules together. Enzymes secreted include lipase, which, along with bile, digests fat; amylases, which break down starch molecules into smaller sugars; and protease, which breaks protein molecules into di-peptide and some single amino acids. In addition to chymotrypsin, other protease enzymes secreted by the pancreas include trypsin and carboxypeptidase.

Chymotrypsin, as a hydrolase type of enzyme (which means it adds a water molecule during the breakdown process) acts by catalyzing the hydrolysis of peptide bonds of proteins in the small intestine. It is selective for peptide bonds with aromatic or large hydrophobic side chains on the carboxyl side of this bond. Chymotrypsin also catalyzes the hydrolysis of ester bonds. Chymotrypsin does not digest blood proteins because of protective factors in the blood that block the enzyme.

General Use

Generally, the primary uses of chymotrypsin are as a digestive aid and as an anti-inflammatory agent. The presence and amount of chymotrypsin in a person's stool is sometimes measured for diagnostic purposes as a test of pancreatic function. Testing for fecal chymotrypsin is non-invasive, unlike some other tests of pancreatic function.

Chymotrypsin, along with the other pancreatic enzymes, is most often used in the treatment of pancreatic insufficiency. Pancreatic insufficiency is characterized by impaired digestion, malabsorption and passing of undigested food into the stool, nutrient deficiencies, gas, and abdominal bloating and discomfort. Pancreatic deficiency also occurs in persons with cystic fibrosis, a rare inherited disorder. It may also occur in those with chronic pancreatitis, as well as in the elderly. Other conditions that could result in chymotrypsin deficiency include physical injuries, chemotherapy, and chronic stress.

Starch and fat digestion can be accomplished without the help of pancreatic enzymes; however, the protease enzymes (i.e., chymotrypsin, trypsin, and carboxypeptidase) are required for proper protein digestion. Incomplete digestion of proteins may result in the development of allergies and the formation of toxic substances produced by putrefaction, the breakdown of protein materials by bacteria. Protease enzymes and other intestinal secretions are also required to keep the small intestine free from parasites such as bacteria, yeast, protozoa, and intestinal worms. A laboratory analysis of a stool sample along with physical symptoms are used to assess pancreatic function.

As an anti-inflammatory agent, the chymotrypsin and the other protease enzymes prevent tissue damage during inflammation and the formation of fibrin clots. Protease enzymes participate in the breakdown of fibrin in a process called fibrinolysis. Fibrin causes a wall to form around an area of inflammation, resulting in the blockage of blood and lymph vessels, which leads to swelling. Fibrin can also cause the development of blood clots. In autoimmune diseases, the protease enzymes aid in the breakdown of immune complexes, which are antibodies produced by the immune system associated with the compounds they bind to (antigens). High levels of immune complexes in the blood are associated with autoimmune diseases.

Specifically, chymotrypsin is used to:

Rutosid (Rutin)

Rutosid, which is more commonly known as Rutin but also called quercetin-3-rutinoside and sophorin, is a bioflavonoid obtained from buckwheat, flower buds of the pagoda tree and the leaves of several species of the Eucalyptus. Rutin is actually a form of Quercetin. Quercetin, one of the most common and abundant flavonoids, occurs bound to sugars in the form known as Rutin or Rutoside. Rutin is generally found in apples, onions, and tea among others. This ingredient is said to strengthen capillaries, as well as lower "bad" cholesterol and reduce the incidence of heart disease in humans.

A flavonol glycoside comprised of the flavonol quercetin. Rutin may have antioxidant, anti-inflammatory, anticarcinogenic, antithrombotic, cytoprotective and vasoprotective activities.

Rutin is a yellow crystalline flavonol glycoside (C27H30O16) that occurs in various plants (rue, tobacco, buckwheat, etc.). Upon hydrolysis (a chemical reaction that uses water to break down a compound), rutin yields quercetin and rutinose.

Rutin is used in many countries as a vasoprotectant and is an ingredient in numerous multivitamin preparations and herbal remedies. The rutosides are naturally occurring flavonoids that have documented effects on capillary permeability and edema (swelling) and have been used for the treatment of disorders of the venous and microcirculatory systems.

There is some evidence for the use of rutin for chronic venous insufficiency, edema, hemorrhoids, microangiopathy (disease of small blood vessels), varicosis and venous disorders. Well presented clinical trials are required in these fields before solid recommendations can be made.

Formulations, mainly consisting of the trihydroxyethyl derivative of rutin, are used in Europe, Mexico and other Latin American countries for the treatment of such venous disorders as varicose veins and hemorrhoids.

Suggested Use

The suggested adult usage for Wobenzym is three tablets, two times daily. Wobenzym should be taken at least 45 minutes before meals. For those who have had health problems or are on any other medication, it would be wise to start with smaller doses of Wobenzym to ensure there is no harmful reaction. You should always consult with your physician before taking any supplements or medication.

Side Effects of Wobenzym N

Wobenzym has no known, negative, side effects. At this time, research has indicated that it is natural and safe. However, patients taking any kind of blood thinners or anti-coagulation drugs should consult with a physician before taking Wobenzym. It is always safest to discuss any supplements or medications you are considering with your physician.

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