An enzyme that breaks down proteins into amino acids
Protease are called proteolytic enzymes or proteinases.
Protease refers to a group of enzymes also called proteolytic enzymes or proteinases whose primary function is the breakdown (catabolism by hydrolysis) of specific peptide bonds (the amino acid links) of amino acids and proteins in a polypeptide chain. This enzyme breaks down proteins into amino acids in a pH range of 4-10. This means that it is active in the “predigestion” stage, inactivates in the lower stomach and reactivates in the small intestine. Aids in the breakdown of undigested proteins that will rot or putrify in the intestinal tract.
Activates white blood cells, breaks down uric acid crystals, supports the liver and reduces spicules, separates red blood cells (protein linkage, rouleau, erythrocyte aggregation). When active in a pH range of 1-5, it is active in the lower portion of the stomach, when pepsin is also active.
rotease are a group of enzymes whose catalytic function is to hydrolyze (breakdown) peptide bonds of proteins, called proteolytic enzymes or proteinases. Proteases differ in their ability to hydrolyze various peptide bonds. Each type of protease has a specific kind of peptide bonds it breaks. Examples of proteases include: fungal protease, pepsin, trypsin, chymotrypsin, papain, bromelain, and subtilisin.
Proteolytic enzymes are very important in digestion as they breakdown the the peptide bonds in the protein foods to liberate the amino acids needed by the body.
Proteolytic enzymes have been used for a long time in 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 rheology control, and immune regulation.
Contrary to old beliefs several studies have shown that orally ingested enzymes can bypass the conditions of the GI tract and be absorbed into the blood stream while still maintaining their enzymatic activity. Commercially, proteases are produced in highly controlled aseptic conditions for food supplementation and systemic enzyme therapy. The organisms most often used are Aspergillus niger and oryzae.
Protease is able to hydrolyze almost all proteins as long as that are not components of living cells. Normal living cells are protected against lysis by the inhibitor mechanism.
Parasites, fungal forms, and bacteria are protein. Viruses are cell parasites consisting of nucleic acids covered by a protein film. Enzymes can break down undigested protein, cellular debris, and toxins in the blood, sparing the immune system this task. The immune system can then concentrate its full action on the bacterial or parasitic invasion.
Protease Deficiency Can Affect Your Health
Acidity is created through the digestion of protein. Therefore a protease
deficiency results in an alkaline excess in the blood. This
alkaline environment can cause anxiety and insomnia.
addition, since protein is required to carry protein-bound calcium
in the blood, a protease deficiency lays the foundation for arthritis,
osteoporosis and other calcium-deficient diseases.
protein is converted to glucose upon demand, inadequate protein
digestion leads to hypoglycemia, resulting in moodiness, mood swings
Protease has an ability to digest unwanted debris in the blood including
certain bacteria and viruses. Therefore, protease deficient people
are immune compromised, making them susceptible to bacterial, viral
and yeast infections and a general decrease in immunity
Proteases As Scavengers of Oxidized and Damaged Proteins Oxidative reactions generate free radical damage 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 free radical damage is minimized. However, in many instances, the body is overwhelmed by the load of proóoxidants (free radical generating molecules), resulting in oxidative stress.
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 proteolysis. For instance, oxidized proteins in blood or extra cellular 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 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. The 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 reduced by an antioxidant enzyme or vitamin to their normal (native) form, or removed 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 Alpha2-macroglobulin. The binding of the Alpha2-macroglobulin to proteases does not inactivate the proteolytic activity of the protease. However, the complexing of the Alpha2-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 hydrolyze and remove extra cellular proteins damaged by free radicals, which are especially susceptible to proteolysis, as mentioned above.
Heavy Metal and Oral Fungal Protease
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 bound to an essential functional protein, (enzymes), they denature and/or inhibit their action. This interaction of heavy metals to proteins can lead to degenerating diseases, nerve damage or even death.
In Studies: Clinical observations have noted that upon high intake of oral protease, heavy metal concentrations have been significantly decreased in the blood. Binding of protease to Alpha2-macroglobulin leads to activated complex with altered binding affinities and an increased rate of clearance from the blood by the liver. It is possible that the activated (Alpha2- macroglobulin protease complex has a high affinity for heavy metals, leading to their removal from the body.
Proteolytic Enzymes Protease is important in digestion as they breakdown protien to liberate the amino acids needed by the body. Proteolytic enzymes have been used in various forms of therapy and studies are indicating their system-wide benefits in oncology, inflammatory conditions, blood flow control, and immune regulation. If taken on an empty stomach, orally ingested enzymes can bypass the GI tract and be absorbed into the blood stream where they can greatly assist the body by acting as a natural anti-inflammatory, natural blood cleanser, virus fighter, and combatant of scarring (fibrin). testing
Proteases are involved in splitting the peptide bonds which link the amino acid residues (elementary units of PROTEINS). Thus proteins are the SUBSTRATES for proteases. These enzymes "digest" long protein chain to shorter fragments. Some of them can detach the terminal amino acids from the protein chain (EXOPEPTIDASES - like aminopeptidases, carboxipeptidase A), the others "attack" internal peptide bonds of a protein (ENDOPEPTIDASES - like trypsin, chymotrypsin, pepsin, papain, elastase).
Proteases are divided into four major groups according to the character of their active site (catalytic site) and conditions of action: serine proteinases, cysteine (thiol) proteinases, aspartic proteinases and METALLOPROTEINASES. Attachment of a protease to a certain group depends on the structure of catalytic site and the amino acid (as one of the consituents) essential for its activity.
Proteases are everywhere and they are involved in various metabolic processes. Acid proteases secreted into the stomach (such as PEPSIN) and serine proteases present in duodeum (TRYPSIN, CHYMOTRYPSIN), enable us to digest the protein in food, proteases present in blood serum (THROMBIN, PLASMIN, HAGEMAN FACTOR etc.) play important role in blood clotting, as well as lysis of the clots, and the correct action of the immune system. Other proteases are present in leukocytes (ELASTASE, CATHEPSIN G) and play several different roles in metabolic control. Proteases determine the lifetime of other proteins playing important physiological role like hormones, antibodies, or other enzymes - this is one of the fastest "switching on" and "switching off" regulatory mechanisms in the physiology of an organism. By complex cooperative action the proteases may proceed as "cascade" reactions which result in amplification of the organism response to the physiological signal, and make this response very fast.
Sources: Aspergillus oryzae,Aspergillus niger
Signs or Symptoms of a Deficiency: Many food allergies are often not much more then a lack of appropriate enzymes. Abdominal pain
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