Enzymes

Protease | Bromelain | Papain | Nattozimes | Trypsin

Amylase | Lactase | Cellulase | Chymotrypsin | Tracite

Protease is responsible for digesting proteins in your food, which is probably one of the most difficult substances to metabolize. Because of this, protease is considered to be one of the most important enzymes that we have. If the digestive process is incomplete, undigested protein can wind up in your circulatory system, as well as in other parts of your body.

When you take protease in higher quantities, it can help to clean up your body by removing the unwanted protein from your circulatory system. This will help to clean up your blood stream, and restore your energy and balance.

One of the tricks of an invading organism is to wrap itself in a large protein shell that the body would view as being "normal". Large amounts of protease can help to remove this protein shell, and allow the body's defense mechanisms can go into action. With the protective barrier down, your immune system can step in and destroy the invading organism.

Additional amounts of protease are also helpful in fighting such things as colds, flu's, and cancerous tumor growths. Protease helps in the healing and recovery from cancer by dissolving the fibrin coating on cancer cells, and thereby giving your immune system a chance to do its job. It can effectively shrink these tumors by helping to remove the dead and abnormal tissues, and by stimulating healthy tissue growth.

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 differ in their ability to hydrolyze various peptide bonds. Each type of protease has a specific kind of peptide bond 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 protein in foods to liberate the amino acids needed by the body. Additionally, 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.

Protease | Bromelain | Papain | Nattozimes | Trypsin

Amylase | Lactase | Cellulase | Chymotrypsin | Tracite

Bromelain is a protein-digesting enzyme complex derived from the stem of the pineapple plant (Ananas comusus)Pineapple has been used medicinally by natives of the tropics for centuries as a digestive aid and wound healer. Current research is confirming its traditional use, finding that bromelain may have numerous health benefits, including anti-inflammatory, wound-healing, digestive, antidiarrheal, immunomodulatory, and anticancer effects. Bromelain is comprised of proteolytic enzymes or cysteine proteases, which hydrolyze proteins to oligopeptides and amino acids. They also exert proteolytic activity at cell surfaces, thereby altering receptor-ligand interactions. Research suggests that bromelain may relieve inflammation by blocking the production of fibrin and kinin, inflammatory compounds which increase swelling and cause pain. It is theorized that bromelain may also improve immunity by increasing production of interferon (a compound that inhibits the replication of viruses), Tumor Necrosis Factor (proteins that help destroy cancer cells), interleukin, and T- immune cells. Bromelain is used for its anti-inflammatory benefits for conditions such as arthritis, injuries, and surgical wounds. Studies suggest that bromelain supplementation may reduce the pain and inflammation associated with arthritis. Other studies show that bromelain may speed healing and reduce pain associated with injuries, burns, and surgical procedures. Bromelain is reported to be effective in treating sports injuries (trauma) as well. One study found a decrease in pain and swelling in 59 patients with musculoskeletal injuries when treated with bromelain. Bromelain is used to support cardiovascular health by reducing risk factors for heart attack and/or stroke. Studies show that bromelain may inhibit platelet aggregation and possibly decrease the pain and inflammation associated with blood clots; improving some symptoms of angina and thrombophlebitis. Bromelain is used as a digestive aid for various digestive disorders such as diarrhea, stomach ulcers, gout, and pancreatic insufficiency. Experimental studies have shown that bromelain also possesses antidiarrheal effects and inhibits activity of the enterotoxins Escherichia coli and Vibrio cholerae. Bromelain is also used in the treatment of upper respiratory tract infections (e.g. chronic bronchitis and acute sinusitis). Bromelain has been shown to have an antitussive effect (cough suppression) and mucolyic activity (reducing the thickness of mucus and bronchial secretions), making it effective in treating respiratory tract diseases. One study in particular demonstrated therapeutic effects in 87% of sinusitis patients treated with bromelain, compared with 68% of sinusitis patients treated with placebo. Bromelain may provide anticancerous effects by inhibiting cancerous tumors. A clinical study in mice found that bromelain decreased lung metastases of Lewis lung cancer cells. Another study of 16 breast cancer patients also demonstrated the therapeutic effects of bromelain, when treated with an oral form. Bromelain may have certain immune-enhancing effects and may boost the effectiveness of certain antibiotics. Therapeutic effects in experimental allergic encephalomyelitis patients were noted when treated with bromelain, trypsin, and the flavonoid rutin, in study. Bromelain may be helpful for women in the treatment of dysmenorrhea and breast engorgement during lactation. Researchers hypothesize that bromelain may have smooth-muscle relaxant effects on the uterus due to prostaglandin modulation. Bromelain should not be taken by individuals allergic to pineapples, honeybee stings, or olive pollen. Pregnant, lactating women and children should not take supplemental bromelain, unless recommended by a health care provider. Side effects may include gastrointestinal symptoms, such as nausea, vomiting, diarrhea, and cramping, as well as metrorrhagia and menorrhagia. Bromelain may enhance activity of some drugs such as anticoagulants (warfarin), antithrombotic agents (aspirin), and antibiotics (amoxicillin, tetracycline). Individuals taking these drugs should exercise caution in the use of bromelain. Bromelain may also have blood-thinning effects.

Protease | Bromelain | Papain | Nattozimes | Trypsin

Amylase | Lactase | Cellulase | Chymotrypsin | Tracite

Papain is a mixture of proteolytic enzymes derived from the juice of the unripe fruit of the tropical plant Caroica papaya, commonly known as papaya. Papain hydrolyzes proteins to form oligopeptides and amino acids. Papain also contains the proteolytic enzyme chymopapain which differs from papain in electrophoretic mobility, solubility and substrate specificity. The molecular weight of chymopapain is approximately 27,000 daltons. Papain is used as a digestive aid. It is also used as a meat tenderizer. Papain has putative anti-inflammatory activity. The activity of papain is expressed in papain units or PU. The assay of papain activity is based on the hydrolysis of casein. Pancreatin enzymes have two important functions in the body: digestion of foods and routine cancer eradication. Pancreatin is a mix of many different enzymes, and those involved in the digestion of proteins are also used to help eliminate cancers that occur. Cancer is often a disease of protein metabolism because the pancreatin enzyme cancer defense mechanism can be overwhelmed by consuming protein rich foods at inappropriate times or in excessive amounts. The body needs a time span each day approaching twelve hours or more without protein consumption for its pancreatin cancer defense mechanism to work optimally. Pancreatin enzymes can be made ineffective by contact with acids or alcohols. A diet comprised mostly of refined foods and meats may result in an acidic body chemistry that depletes these enzymes. Cancer, once established, ensures its survival by continuously generating acid as it inefficiently metabolizes food. Consuming alcoholic beverages can also interfere with the defense mechanism. Many popular cosmetics that contain acids or alcohols are a special concern for skin cancer. Mercury leakage from amalgam tooth fillings is also debilitating to many enzyme functions. Papain is a proteolytic (protein degrading) enzyme, characterized by the ability to hydrolyze large proteins into smaller peptides and amino acids. Its broad substrate specificity and ability to hydrolyze small peptides as well as large proteins make Papain an ideal enzymatic supplement.

Protease | Bromelain | Papain | Nattozimes | Trypsin

Amylase | Lactase | Cellulase | Chymotrypsin | Tracite

Nattozimes™ is helpful in the prevention and resolution of excessive clotting and disorders resulting from excessive clotting. Similar to products used extensively in Japan, Nattozimes™ helps to reduce high blood pressure. Natto is fermented soybeans that have been a traditional Japanese staple for more than 1,000 years. Its' medical benefits are widely recognized in Japan, resulting in its increased popularity. Some of the effects are attributed to its soybean origin. Bacillus Natto produces various enzymes, vitamins, amino acids and other nutrients unique to Natto during its fermentation. It is these unique elements that give Natto its distinctive health and medical benefits. Nattokinase and Pyrazine may prevent or resolve blood clots.

Proteases have been extensively studied since the 1960’s for their Fibrinolytic and Antithrombic effects. Many have shown great potential to improve blood fluidity and reduce platelet aggregation. Nattozimes™ is specifically formulated to support the body in breaking up and dissolving unhealthy coagulation of blood and to support Fibrinolytic activity. Nattozimes is a proprietary fungal Proteolytic enzyme blend that matches the unique Fibrinolytic activity of the Natto fermentation process. Studies show the same Thrombolytic and Fibrinolytic activities as Nattokinase, which makes Nattozimes™ a 1 to 1 alternative for Nattokinase for cardiovascular and anti-inflammatory support.

Nattokinase has been used in Japan to treat heart disease and inflammatory disease for over twenty years. The fibrinolytic and antithrombic activities of nattokinase explain these applications. Nattozimes® exhibits these same activities in vitro, demonstrating that Nattozimes® is an excellent substitute for nattokinase in supplements intended to provide cardiovascular or anti-inflammatory support. In vitro, animal studies, and human trials have demonstrated that nattokinase has powerful antithrombic activity (Sumi et al, 1987)(Sumi et al, 1990)(Fujita et al, 1993)(Fujita et al, 1995). In vitro studies clearly show that nattokinase not only actively degrades plasmin and fibrin, important components of thrombi, but that its actions are longer lasting than some standard antithrombic therapies (Sumi et al, 1987)(Fujita et al, 1993). These in vitro findings were further supported by animal models which showed that not only could nattokinase be absorbed through the intestinal tract, but that it acts to dissolve experimental blood clots in vivo (Sumi et al, 1990)(Fujita et al, 1995). Human trials performed by Daiwa Pharmaceutical Company confirmed that previous findings are also applicable to human subjects (http://www.daiwa-pharm.com). While the findings for nattokinase are impressive, it is not the only protease shown to be beneficial for the use in cardiovascular support. Proteases have been extensively studied, since the 1960’s, for their fibrinolytic and antithrombic effects, and many have shown great potential to improve blood fluidity and reduce platelet aggregation (Maurer, 2001)(Larsson et al, 1988)(Taussig and Batkin, 1988)(Felton, 1980). Of particular interest, proteases from Aspergillus oryzae have been shown to form complexes with alpha 2-macroglobulins. These complexes have powerful antithrombic effects, in vivo (Larsson et al, 1988).

Protease | Bromelain | Papain | Nattozimes | Trypsin

Amylase | Lactase | Cellulase | Chymotrypsin | Tracite

Trypsin and chymotrypsin, like most proleotytic enzymes, are synthesized as inactive zymogen precursors (trypsinogen and chymotrypsinogen) to prevent unwanted destruction of cellular proteins, and to regulate when and where enzyme activity occurs. The inactive zymogens are secreted into the duodenum, where they travel the small and large intestines prior to excretion. Zymogens also enter the bloodstream, where they can be detected in serum prior to excretion in urine. Zymogens are converted to the mature, active enzyme by proteolysis to split off a pro-peptide, either in a subcellular compartment or in an extracellular space where they are required for digestion.

Trypsin and chymotrypsin are structurally very similar, although they recognise different substrates. Trypsin acts on lysine and arginine residues, while chymotrypsin acts on large hydrophobic residues such as tryptophan, tyrosine and phenylalanine, both with extraordinary catalytic efficiency. Both enzymes have a catalytic triad of serine, histidine and aspartate within the S1 binding pocket, although the hydrophobic nature of this pocket varies between the two, as do other structural interactions beyond the S1 pocket.

The human pancreas secretes three isoforms of trypsinogen: cationic (trypsinogen-1), anionic (trypsinogen-2) and mesotrypsinogen (trypsinogen-3). Cationic and anionic trypsins are the major isoforms responsible for digestive protein degradation, occurring in a ratio of 2:1, while mesotrypsinogen accounts for less than 5% of pancreatic secretions. Mesotrypsin is a specialised protease known for its resistance to trypsin inhibitors. It is thought to play a special role in the degradation of trypsin inhibitors, possibly to aid in the digestion of inhibitor-rich foods such as soybeans and lima beans. An alternatively spliced mesotrypsinogen in which the signal peptide is replaced with a different exon 1 is expressed in the human brain; the function of this brain trypsinogen is unknown.

Protease | Bromelain | Papain | Nattozimes | Trypsin

Amylase | Lactase | Cellulase | Chymotrypsin | Tracite

Amylase, an enzyme having physiological, commercial, and historical significance, also called diastase. It is found in both plants and animals. Amylase was purified (1835) from malt by Anselme Payen and Jean Persoz. Their work led them to suspect that similar substances, now known as enzymes, might be involved in biochemical processes. Amylase hydrolyzes starch, glycogen, and dextrin to form in all three instances glucose, maltose, and the limit-dextrins. Salivary amylase is known as ptyalin; although humans have this enzyme in their saliva, some mammals, such as horses, dogs, and cats, do not. Ptyalin begins polysaccharide digestion in the mouth; the process is completed in the small intestine by the pancreatic amylase, sometimes called amylopsin. The amylase of malt digests barley starch to the disaccharides that are attacked by yeast in the fermentation process.
Enzymes are a class of proteins which catalyse chemical reactions. Unlike nonbiological catalysts such as charcoal and platinum, which often need harsh extremes of temperature and pH, enzymes must work in the mild conditions of a cell in the body, at approximately 40oC and at a pH between 6.5 and 7.5. When compared with inorganic catalysts, enzymes are different in their rate of reaction (often 106 to 1012 the rate of the uncatalysed reaction) and in their specificity, their ability to act selectively on a small group of chemically similar substances. Chemicals changed by enzyme-catalysed reactions are called the substrates of that enzyme, and they fit into the active site of the enzyme, where the reaction takes place, in a lock-and-key mechanism. The products of the reaction then leave the active site, freeing it up for more similar reactions to take place.
Carbohydrates are one of the three major food groups needed for proper nutrition. Amylase is the digestive enzyme needed to digest carbohydrates. It is a well known fact that cancer feeds on sugars, mainly refined sugars like dextrose, sucrose, dextrin, etc... Cancer needs sugar as it's main source of energy which it gets through the blood supply or ultimately by ingestion. An intake of amylase will keep carbs, especially those used by cancer, to a minimum or yield a converted substance which the body will use. Sugars also cause acid formation which this enzyme helps to reduce.

Protease | Bromelain | Papain | Nattozimes | Trypsin

Amylase | Lactase | Cellulase | Chymotrypsin | Tracite

Lactase is an enzyme that breaks down the milk sugar lactose into glucose and galactose. Persons with a deficiency of lactase in the gut can develop abdominal cramping and diarrhea after ingesting milk products.

It has been known for decades that cancer cells produce excessive amounts of lactic acid. The fact that most cancers have poor vascular systems has led cancer scientists to assume that such cells are deprived of a normal supply of oxygen. Researchers believe that without sufficient oxygen, cancer cells must revert to fermentation for their energy supply and this is what causes them to produce excessive lactic acid. I challenge this traditional assumption and suggest instead that cancer cells have dysfunctional mitochondria, which prevent their use of the citric acid cycle. Consequently, pyruvic acid, the normal end product of glycolysis, which normally would enter the mitochondria for its total combustion into energy, is instead converted to lactic acid. Evidence exists to support this hypothesis which, when acknowledged, could dynamically impact both cancer research and the treatment of all forms of cancer.

It is reported that cancer cells can produce forty times more lactic acid than normal cells. Many primitive life forms cannot survive in an oxygen environment and therefore derive their energy from fermentation. In this process they normally produce inordinate amounts of lactic acid. Cancer scientists have assumed that since cancer cells usually have poor vascular systems, they lack oxygen and therefore revert to fermentation for their major source of energy. Researchers believe it is the lack of oxygen that causes cancer cells to produce excessive lactic acid.

Since cancer already creates large amounts of Lactic acid it is a good idea keep lactase in the system to break down lactose. Lactic Acid can result from too much Lactose in one's system. Person's with cancer should be careful not to consume too much mucous rich foods such as dairy. Mucous can impair immune response and cause sinus problems.

Protease | Bromelain | Papain | Nattozimes | Trypsin

Amylase | Lactase | Cellulase | Chymotrypsin | Tracite

Cellulase is an enzyme which breaks down cellulose. Cellulose is an indigestible plant polysaccharide. It is the principal constituent of the cell wall of plants. Cellulase has cellulolytic activity, meaning that it hydrolyzes cellulose. Cellulase hydrolyzes the beta-D-1, 4-glycosidic bonds of cellulose. Cellulase enzymes show activity during the ripening of some fruits, where their effects on cell walls results in softening of the fruit. The vital characteristics of this cellulase complex are 1) the system is multienzymatic; 2) at least three enzyme components are both physically and chemically distinct; and 3) all three components play essential roles in the hydrolysis of cellulose to glucose. The assay for cellulase activity uses a method which determines the effect of cellulase on microcrystalline cellulose with respect to glucose formation. Released glucose is determined in a hexokinase/glucose-6-phosphate dehydrogenase system at 340 nm.

Cellulase is an enzyme that breaks down cellulose, the carbohydrate that is the main part of the cell walls of plants. Cellulose is nondigestible by humans because we to not produce the enzyme cellulase. Cellulase is produced by grazing animals such as cows (with the aid of the beneficial bacteria that reside in the animal's digestive tract), and is the reason why they can get nutrition from plants such as grasses. The human body does not produce cellulase, however, it is available for supplementation since it can help us break down plant material better, thereby getting the most from the plants that we eat.

Protease | Bromelain | Papain | Nattozimes | Trypsin

Amylase | Lactase | Cellulase | Chymotrypsin | Tracite

Chymotrypsin, proteolytic, or protein-digesting, enzyme active in the mammalian intestinal tract. It catalyzes the hydrolysis of proteins, degrading them into smaller molecules called peptides. Peptides are further split into free amino acids. Chymotrypsin is produced in the pancreas as the inactive, or zymogen, form chymotrypsinogen. Along with other digestive enzymes of the pancreas, chymotrypsinogen is carried in the pancreatic juice through the pancreatic duct into the duodenum. There chymotrypsinogen is activated by another enzyme, trypsin, and by molecules of active chymotrypsin.

Together, trypsin and chymotrypsin are also known to be powerful inhibitors of cancer and are considered to be the body's natural "cancer fighters". Scientists at Johns Hopkins and Tsukuba University in Japan have confirmed this. Researcher Paul Talalay, M.D stated that:

"20 years of research confirms that raising the levels of phase II enzymes [glutathione, trypsin and chymotrypsin] can offer a highly effective way to achieve protection against carcinogenesis (development of new cancer)".

This potent inhibition action of phase II enzymes is not hard to explain. Phase II enzymes fight cancers by destroying "trophoblast cells". These cells act as a protective shell to cancer by shielding it from our immune system, thus allowing it to proliferate. Without this protective shell cancer becomes an easy target for the body's immune system to destroy.

Protease | Bromelain | Papain | Nattozimes | Trypsin

Amylase | Lactase | Cellulase | Chymotrypsin | Tracite

Almost every disease, sickness or ailment can be traced to a mineral deficiency. ~Dr. Linus Pauling. Tracite is a highly bio-available, iron-based source of 77 essential minerals and trace elements. Tracite is composed of Ancient organic plant matter derived from humic shale. The fulvic minerals are extracted from the shale using our proprietary pure water method, with absolutely no chemicals or acids used in the process of extraction. Tracite contains more electrolytes than most other products available on the market. The high fulvic acid content of Tracite gives it some unique electrical properties. Every cell in the body depends on fulvic, colloidal trace minerals and elements for that daily trickle charge of bio-electrical energy and independent tests have shown that Tracite has excellent conductivity. Tracite contains both ionic and colloidal particles. When combined with enzymes (see Flora-Zymes), the minerals and trace elements in Tracite form alkalizing detoxifying agents, which neutralize acid and other metabolic by-products, preparing them for elimination. Tracite contains the minerals and trace elements your body needs to keep toxins from accumulating. Some of the immediate benefits of taking Tracite fulvic minerals include increased stamina and endurance, improved mental clarity and physical well-being, and more beautiful skin, hair and nails. Tracite is the best iron supplement available and it greatly increases the bodies ability to absorb nutrients into the cells. It is the only mineral supplement of its kind in the world.