Amylase, Lipase, Protease and Cellulase
NOTE: For optimum results when using enzymes a readily absorbable calcium and lactobacilli micro cultures should be taken. (Commensal Bio-Cultures is he most effective and comprehensive micro culture product we have found.
Amylase enzymes hydrolyze or digest large polysaccharide molecules, commonly known as carbohydrates, into small disaccharide molecules, which are eventually reduced to the monosaccharide, glucose, before reaching the cell. Glucose is one of the primary raw materials used by the body in the production of energy. The mitochondria in the cells transform glucose into Adenosine Triphosphate (ATP), a high-energy compound that releases its energy to facilitate cellular function. Therefore, when the body is deficient in amylase enzymes, it is also deficient in its main source of energy, glucose.
According to the Gell and Coombs classification of hypersensitivity reactions, Type I reactions result from the release of pharmacologically-active substances, such as: histamine, serotonin, slow reacting substance of anaphylaxis (SRS-A) and eosinophilic chemotactic factor of anaphylaxis (ECF-A), from 1gE-sensitized basophils and mast cells after contact with a specific antigen. These released substances cause vasodilation, increased capillary permeability, smooth muscle contractions and eosinophilia. This inflammatory response is usually manifested in those organ systems of the body, which come in contact with the outside world, most notably the respiratory tract and the skin. Some of the clinical conditions in which Type I reactions play a role, include: seasonal allergic rhinitis (hayfever), extrinsic asthma, atopic dermatitis and urticaria/angioedema. Inflammation caused by the release of histamine and similar substances can also be triggered by trauma and acute or chronic infections.
The pharmacologically active substances that cause an inflammatory response are stored in the granules of mast cells or basophils until a stimulus prompts their release. Neurohormones modulate the release of these substances. The function of these neurohormone is controlled by cAMP and cGMP systems within the cells. The intracellular concentration of cAMP is a principal determinant of both the inhibition of the release of several chemical mediators, such as histamine, and the relaxation of the smooth muscles. The production of cAMP and cGMP requires adequate ATP as a precursor. Therefore, when there is a deficiency of ATP in the cell, insufficient cAMP and cGMP will be produced, causing imbalances in the neurohormone control of inflammation. In a study reported in Health and Longevity, a significant number of patients, exhibiting skin conditions, such as dermatitis, were found to have low blood levels of amylase. High-potency amylase enzymes , taken between meals, will be absorbed into the bloodstream to affect the digestion of carbohydrates, providing glucose for the production of ATP; and its subsequent conversion to cAMP and cGMP.
In addition, amylase in the bloodstream may contribute to the immunological attack on certain myxoviruses which are enveloped in a coat composed principally of glycoproteins (proteins bound to carbohydrates). These myxoviruses are known to cause acute respiratory conditions and skin eruptions.
Amylase enzymes hydrolyze large carbohydrate molecules into smaller disaccharides. If carbohydrates are not properly digested, they cannot be utilized by the body to:
Most of the bile acids, excreted in the bile, are reabsorbed through the intestinal mucosa. Some of this reabsorption is affected by bacterial action in the colon. Another constituent of bile, bilirubin, is converted by intestinal bacteria to urobilinogen. Unlike bilirubin, this urobilinogen is water-soluble and is, therefore, transported to the liver for re-excretion in the bile. Lactobacillus Acidophilus is the most prevalent bacteria found in the lower intestines and plays a major role in the recycling of bile components. Maintaining healthy intestinal flora is imperative to normal bile production and subsequent fat digestion.
In the digestive process, exogenous lipase enzymes will aid pancreatic lipase and bile in breaking down dietary fats. Those individuals experiencing biliary problems should gradually improve their digestion and absorption of dietary fat through the use of moderate amounts of supplemental lipase. Flooding the body with fatty acids from the diet can have a detrimental effect if all aspects of fat metabolism and bile production have not been normalized. In addition to amylase and lipase, protease and cellulase are provided to help utilize other important food nutrients.
Lipase enzymes hydrolyze neutral fat (triglycerides) into diglycerides, monoglycerides and, finally, glycerol and free fatty acids. Human and animal studies have provided irrefutable evidence that lipolytic enzymes, preferably taken on an empty stomach, can and are absorbed intact, from the gastrointestinal tract into the bloodstream, under normal conditions. These lipases increase the lipolytic activity of the blood, helping the body dispose of undesirable and often detrimental fat in the extra-cellular fluids. In particular, certain extremely resistant organisms responsible for many chronic conditions, have thick lipid membranes that macrophages have been found to digest with lipase enzymes.
Lipase enzymes in the body play an important role in fat metabolism. Theoretically, most of the dietary fat that is absorbed into the body has been properly digested in the gastrointestinal tract, yet, studies indicate undigested fat is absorbed in appreciable quantities. There are two principle mechanisms by which fat is absorbed. Short chain fatty acids, such as those in butterfat, are absorbed directly into the blood through the capillary system in the epithelial cells of the intestines and transported throughout the body, attached to blood protein albumin. Long chain fatty acids, monoglycerides and diglycerides are resynthesized into new triglycerides in the intestinal wall, combined with cholesterol and phospholipids, then partially surrounded with protein forming chylomicrons. These chylomicrons are dumped into the lymph, where it is transported up to the thoracic duct and emptied into the venous blood. After a meal high in fat, the lymph in the thoracic duct appears milky, due to the water-insoluble fat. Once in the plasma, the chylomicrons are rapidly removed from the circulating blood, as it passes through the capillaries of adipose and liver tissue. These tissues contain large amounts of lipolytic enzymes to break down the chylomicrons. Undigested triglycerides and diglycerides are highly soluble in the lipid membrane of the epithelial cell, and even though bile does not assist in their absorption, a diet high in fat is likely to result in considerable undigested fat being absorbed into the blood and lymph. There is some speculation that absorption of unhydrolyzed fat may contribute to hardening of the arteries. Lipase in the extracellular fluid can break down large fat molecules into biochemically useful free fatty acids.
The family of fatty acid derivatives, known as prostaglandins, are potent activators involved in many biological processes---especially inflammation. Research has demonstrated that prostaglandins have a profound effect on: vascular dilation and permeability, platelet aggregation, blood clotting, cholesterol synthesis, blood vessel tone, blood pressure, and the immune system. Proper metabolism of essential fatty acids can affect the type and amount of prostaglandin synthesis in the tissues of the body. There are three main series of prostaglandins that need to be kept in balance, in order to inhibit or reduce symptoms of inflammation.
Although the exact cause of cholesterol deposits on arterial walls is unclear, there is overwhelming evidence that it is associated with how effectively fat is metabolized. Free fatty acids is the preferred form of fat, to be transported to other areas of the body, for use in energy production. However, 95% of the lipids in the blood are in the form of lipoproteins, containing a mixture of triglycerides, phospholipids, cholesterol and protein. There are three major classifications of lipoproteins. Very Low Density Lipoproteins (VLDLs), containing high amounts of triglycerides and moderate amounts of cholesterol, transport triglycerides to peripheral tissue. After most of the triglycerides have been delivered, VLDLs in the blood become Low Density Lipoproteins (LDLs), the molecular complex responsible for depositing cholesterol in the tissues--of major concern, the arteries. High Density Lipoproteins (HDLs) are beneficial, as they transport cholesterol away from tissues back to the liver. Lipase can break down triglycerides into free fatty acids, potentially reducing the VLDL and subsequent LDL levels in the blood. University studies demonstrated blood lipase levels progressively decline in patients exhibiting excessive cholesterol deposits in their arteries, with advancing middle and old age. The results showed the blood of individuals averaging 77 years of age had only half the lipase of an average 27 year old group. Additional studies have shown lipid levels of the blood were lowered when sufficient exogenous lipase was ingested.
Protease enzymes hydrolyze or digest large protein molecules into smaller polypeptides and amino acids. When taken between meals, protease enzymes can be absorbed into the bloodstream. These proteolytic enzymes will help the body dispose of undesirable and often detrimental protein factions in the blood. In particular, this proteolytic activity has been found to help reduce the effects of inflammation. When there is cellular injury, chemical substances are released that initiate the inflammatory process, by increasing blood flow to the area, as well as capillary permeability, so almost pure plasma leaks into the damaged tissue. Leukocytes and macrophages emigrate from the blood vessels into the focus area, where phagocytosis immediately starts. At this time, insoluble fibrin clots also develop at the periphery of the inflamed area, enclosing the destroyed or damaged tissue, which prevents the migration of disease-causing agents or toxins to other areas of the body. The formation of fibrin clots interferes with local circulation, resulting in edema and pain. These symptoms are relieved when proteolytic enzymes, natural to the body, known as plasmin, begin breaking down the fibrin clots into smaller, soluble peptides and amino acids during the reparative process.
Although the immediate fibrin deposit is one of the most important defense mechanisms in the body, an imbalance between the number of fibrin clots formed and the amount of plasmin present, to dissolve the clot, has been found to cause a number of serious pathological processes. This type of imbalance can manifest itself in exaggerated inflammatory symptoms, such as: more extensive edema, more pain, complete stoppage of circulation to the area, a delay of the phagocytic stage of inflammation, and delayed healing with excess scar formation. In a number of animal experiments, it has been shown that the exogenous introduction of protease shortly after an inflammatory irritation, markedly reduced the intercellular and intraarterial fibrin formation, in comparison with normal controls. Fever, as an accompanying symptom of inflammation, is brought on by a thermostable polypeptide, known as pyrexin. Proteolytic enzymes given to human subjects, suffering from inflammation, have also experienced a dramatic resorption of the edemic fluid and relief of the heat, redness, swelling and pain. This type of enzyme therapy has been found to be particularly successful in the treatment of: soft tissue traumas (sports injuries), bone fractures, deep abscesses, gum conditions, respiratory congestion (such as bronchitis), and inflammatory conditions of the throat, nose, mouth, ear and sinuses.
It is known that proteases are able to dissolve almost all native proteins, as long as they are not components of living cells. Normal, living cells are protected against lysis by an inhibitor mechanism. Viruses are cell parasites, consisting of nucleic acids, covered by a protein film, which, in their extracellular phase, do not show any of the characteristics of life. Studies have found that the protein cover of the viruses, during their extracellular phase, can be dissolved, or at least inactivated by proteolytic activity, which leads to a loss of viral infectivity. Therefore, the elevation of the proteolytic enzymes in the blood and plasma, represents an efficient means to control viral infections. This type of therapy has been found to inhibit the infectivity of several types of viruses in man, including six different influenza Type A viruses and cold viruses. Although bacteria and parasites cannot be inactivated directly by exogenous proteolytic enzymes (due to a protective mechanism in their cell membranes), proteolytic enzymes can break down undigested protein, cellular debris and toxins in the blood, sparing the immune system from this task. Consequently, the immune system can concentrate its full action on the bacterial or parasitic invasion.
An inability to properly digest protein also plays a major role in the incidence of other health disorders, such as: hypoglycemia, menopause, PMS and anxiety syndromes. Supplemental proteolytic enzymes will help the body digest proteins so it can be used: to make hormones, as another source of glucose, and to carry calcium to structural components and to the nervous system.
Cellulase The carbohydrate content of the human diet consists, primarily, of four types: sucrose (a disaccharide usually derived from cane or beet, known as refined sugar), lactose (a disaccharide, known as milk sugar), starch (a large polysaccharide, which is stored fuel in plants) and cellulose (a large polysaccharide, which is the main structural component in plants). Ideally, the digestive system breaks these carbohydrates down into the monosaccharide---glucose (80%), fructose (10%), and galactose (10%)---which can be readily absorbed into the bloodstream and utilized by the body.
The brush boarders of the mucosal cells, lining the small intestine (jejunum), secrete digestive enzymes, which finish the digestion of food started earlier in the digestive tract. This final step in the digestive process, renders nutrients small enough to be absorbed into the body through the wall of the small intestine. Among the enzymes secreted by the small intestines, are: sucrase, lactase, and maltase; these enzymes reduce larger carbohydrate molecules into monosaccharides.
The human digestive system does not secrete enzymes capable of breaking down cellulose, so this fibrous carbohydrate moves through the digestive tract, essentially intact, unless the enzyme, cellulase is present in the diet. Cellulase is provided by either raw foods or plant enzyme supplements.
Cellulase digests cellulose into glucose and short chain fatty acids.
A deficiency of one or more of the disaccharide-splitting enzymes--sucrase, lactase, maltase or cellulase---generally leads to diarrhea/constipation, bloating, flatulence, nausea, headache and/or abdominal cramps, after ingestion of foods containing the offending sugar, starch, and/or fiber. The diarrhea is due to the increased number of unsplit disaccharide molecules remaining in the intestinal lumen, which are osmotically retaining fluid. The bloating and flatulence are caused by the production of gas (CO2) and H2), from the bacterial fermentation of the disaccharide residue in the lower small intestine and colon. The excessive amount of sucrose and lactose in the modern diet can exhaust the body's ability to produce sucrase and lactase enzymes. Lactase deficiency is the most recognized of the disaccharide-splitting enzyme deficiencies; however, sucrose deficiencies may explain the increasing inability of many people to handle the sucrose in their diets. Most mammals, including humans, have high intestinal lactase activity at birth. But, in some races, this activity declines to low levels during childhood and remains low in adulthood. The low lactase levels cause an intolerance to milk (lactose intolerance). 75% of American Blacks, 75% of American Indians, 90% of Orientals and 20% of American Caucasians are intolerant to lactose.
Cellulase deficiencies are often overlooked, yet a lack of cellulase can mean poor digestion of raw foods and less than optimal absorption of nutrients in the intestines. Starches in uncooked foods are coated with cellulose, which must be removed before the nutritious value of these substances can be realized. If the food is eaten raw, adequate chewing is required to release the cellulase naturally found in the food. Unfortunately, most people do not chew their food thoroughly enough to release the full digestive benefits of the food cellulase, meaning this food will not be completely digested. Cellulase makes soluble fiber available to the body. Soluble fiber increases intestinal absorption of nutrients and has been recently cited for its beneficial effects on cholesterol levels.
These statements have not been evaluated by the Food and Drug and Administration This information and product is this not intended for use in the diagnosis, cure, mitigation, treatment or prevention of any disease or condition or to encourage the abandonment of conventional therapy.