Prozyme

Systemic Enzymes are complex proteins that stimulate chemical changes in other substances. They work optimally at specific temperature and pH. Digestive enzymes include pancreatic enzymes, plant-derived enzymes, and fungal-derived enzymes. There are three classes of digestive enzymes: proteolytic enzymes needed to digest protein, lipases needed to digest fat, and amylases needed to digest carbohydrates. Only small amounts of the animal-based proteolytic enzymes, trypsin and chymotrypsin, are found in the diet; however, the pancreas can synthesize these enzymes.

A literature review yielded studies beginning with Brendel, et al., in 1956, who demonstrated that trypsin had an anti-inflammatory action when administered buccally.1 In 1957, Martin, et al., showed that when trypsin, chymotrypsin and papain were injected into the small intestines, they were not denatured or digested, but absorbed with enough of the molecules intact to exert marked systemic anti-inflammatory effect. They theorized that enterically coating these substances would enable them to be administered orally.

There were two other interesting findings: proteolytic enzymes ingested on an empty stomach can retain up to 40% of their activity, and proteolytic enzymes appear to have an affinity to accumulate at sites of inflammation.

In 1998, researchers gave bromelain and trypsin at 400 to 800 mg four times a day for four days to 21 people. They found that the plasma levels of both enzymes increased and that these increases correlated with the amount of enzymes supplemented. They concluded that the absorption of large protein molecules of proteolytic enzymes does occur, and they felt this could explain why proteolytic enzymes have been successfully used to treat posttraumatic inflammation, edema and bruising.

Enzyme treatment with systemic enzymes helps to clean the excess fibrin, and reduce the blood cells stickiness. Both will minimize the clots from happening, which is known as the major reason someone gets stroke or heart attack. Systemic enzymes help break down the waste material until they’re small enough to be disposed through the bowel. Clean the receptors of FC in the white blood cells, improve their functions and availability for infection combat.

Pancreatin is a combination of digestive enzymes (proteins). These enzymes are normally produced by the pancreas and are important in the digestion of fats, proteins, and sugars. Pancreatin is used to replace digestive enzymes when the pancreas does not produce enough on its own. Certain medical conditions can cause this lack of enzymes, including cystic fibrosis, chronic inflammation of the pancreas, pancreatic cancer, or pancreas surgery. Pancreatin may also be used to treat a condition called steatorrhea (loose, fatty stools).

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.

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.

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.

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.

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.

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.

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. Orally, chymotrypsin is used for reducing inflammation and edema associated with abscesses, ulcers, surgery or traumatic injuries; as an expectorant in asthma, bronchitis, pulmonary diseases, and sinusitis. It is used in minimizing initial rise in serum liver enzymes in burn patients, reducing liver stress, and associated degradative changes during wound repair. Chymotrypsin, along with the other pancreatic enzymes, is often used in the treatment of pancreatic insufficiency.

Trypsin acts to degrade protein; it is often referred to as a proteolytic enzyme, or proteinase. Trypsin is one of the three principal digestive proteinases, the other two being pepsin and chymotrypsin. In the digestive process, trypsin acts with the other proteinases to break down dietary protein molecules to their component peptides and amino acids. Trypsin continues the process of digestion (begun in the stomach) in the small intestine where a slightly alkaline environment (about pH 8) promotes its maximal enzymatic activity. Trypsin, produced in an inactive form by the pancreas, is remarkably similar in chemical composition and in structure to the other chief pancreatic proteinase, chymotrypsin. Both enzymes also appear to have similar mechanisms of action; residues of histidine and serine are found in the active sites of both. The chief difference between the two molecules seems to be in their specificity, that is, each is active only against the peptide bonds in protein molecules that have carboxyl groups donated by certain amino acids. For trypsin these amino acids are arginine and lysine, for chymotrypsin they are tyrosine, phenylalanine, tryptophan, methionine, and leucine. Trypsin is the most discriminating of all the proteolytic enzymes in terms of the restricted number of chemical bonds that it will attack.

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.