Amylase (English pronunciation: /ˈæmɪleɪz/) is an enzyme that catalyses the breakdown of starch into sugar. Amylase is present in human saliva, where it begins the chemical process of digestion. Foods that contain much starch but little sugar, such as rice and potato, taste slightly sweet as they are chewed because amylase turns some of their starch into sugar in the mouth. The pancreas also makes amylase (alpha amylase) to hydrolyse dietary starch into disaccharides and trisaccharides which are converted by other enzymes to glucose to supply the body with energy. Plants and some bacteria also produce amylase. As diastase, amylase was the first enzyme to be discovered and isolated (by Anselme Payen in 1833). Specific amylase proteins are designated by different Greek letters. All amylases are glycoside hydrolases and act on α-1,4-glycosidic bonds.
Amylase enzymes find use in bread making and to break down complex sugars such as starch (found in flour) into simple sugars. Yeast then feeds on these simple sugars and converts it into the waste products of alcohol and CO2. This imparts flavour and causes the bread to rise. While Amylase enzymes are found naturally in yeast cells, it takes time for the yeast to produce enough of these enzymes to break down significant quantities of starch in the bread. This is the reason for long fermented doughs such as sour dough. Modern bread making techniques have included amylase enzymes (often in the form of malted barley) into bread improver thereby making the bread making process faster and more practical for commercial use.
When used as a food additive Amylase has E number E1100, and may be derived from swine pancreas or mould mushroom.
Bacilliary amylase is also used in clothing and dishwasher detergents to dissolve starches from fabrics and dishes.
Workers in factories that work with amylase for any of the above uses are at increased risk of occupational asthma. 5-9% of bakers have a positive skin test, and a fourth to a third of bakers with breathing problems are hypersensitive to amylase.
An inhibitor of alpha-amylase called phaseolamin has been tested as a potential diet aid.
Blood serum amylase may be measured for purposes of medical diagnosis. A normal concentration is in the range 21-101 U/L. A higher than normal concentration may reflect one of several medical conditions, including acute inflammation of the pancreas (concurrently with the more specific lipase), but also perforated peptic ulcer, torsion of an ovarian cyst, strangulation ileus, macroamylasemia and mumps. Amylase may be measured in other body fluids, including urine and peritoneal fluid.
In molecular biology, the presence of amylase can serve as an additional method of selecting for successful integration of a reporter construct in addition to antibiotic resistance. As reporter genes are flanked by homologous regions of the structural gene for amylase, successful integration will disrupt the amylase gene and prevent starch degradation, which is easily detectable through iodine staining.
Trypsin (EC 126.96.36.199) is a serine protease found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive proenzyme trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or 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, and proteins that have been digested/treated with trypsin are said to have been trypsinized.
Trypsin is secreted into the duodenum, where it acts to hydrolyse peptides into their smaller building-blocks, namely amino acids (these peptides are the result of the enzyme pepsin's breaking down the proteins in the stomach). This enables the uptake of protein in the food because peptides (though smaller than proteins) are too big to be absorbed through the lining of the ileum. Trypsin catalyses the hydrolysis of peptide bonds.
Trypsin is produced in the pancreas in the form of the inactive zymogen trypsinogen. When the pancreas is stimulated by cholecystokinin, it is then secreted into the small intestine. Once in the small intestine, the enzyme enteropeptidase activates it into trypsin by proteolytic cleavage. The resulting trypsins themselves activate more trypsinogens (autocatalysis), so only a small amount of enteropeptidase is necessary to start the reaction. This activation mechanism is common for most serine proteases, and serves to prevent autodigestion of the pancreas.
A lipase is a water-soluble enzyme that catalyzes the hydrolysis of ester chemical bonds in water-insoluble lipid substrates. Lipases are a subclass of the esterases.
Lipases perform essential roles in the digestion, transport and processing of dietary lipids (e.g. triglycerides, fats, oils) in most, if not all, living organisms. Genes encoding lipases are even present in certain viruses.
Most lipases act at a specific position on the glycerol backbone of lipid substrate (A1, A2 or A3)(small intestine). For example, human pancreatic lipase (HPL), which is the main enzyme that breaks down dietary fats in the human digestive system, converts triglyceride substrates found in ingested oils to monoglycerides and free fatty acids.
Several other types of lipase activities exist in nature, such as phospholipases and sphingomyelinases, however these are usually treated separately from "conventional" lipases.
Some lipases are expressed and secreted by pathogenic organisms during the infection. In particular, Candida albicans has a large number of different lipases, possibly reflecting broad lipolytic activity, which may contribute to the persistence and virulence of C. albicans in human tissue.
Protein Digestion by TrypsinTrypsin, an enzyme produced by the pancreas, hydrolyzes proteins to small fragments (proteoses, peptones, and peptides). BAPNA is a synthetic (man-made) protein substrate consisting of a dye covalently bound to an amino acid. Trypsin hydrolysis of BAPNA cleaves the dye molecule from the amino acid, causing the solution to change from colorless to bright yellow. Since the covalent bond between the dye molecule and the amino acid is the same as the peptide bonds that link amino acids together, the appearance of a yellow color indicates the presence and activity of an enzyme that is capable of peptide bond hydrolysis. Because the color change from clear to yellow is direct evidence of hydrolysis, additional tests are not required when determining trypsin activity using BAPNA.
Bile acts to some extent as a surfactant, helping to emulsify the fats in the food. Bile salt anions have a hydrophilic side and a hydrophobic side, and therefore tend to aggregate around droplets of fat (triglycerides and phospholipids) to form micelles, with the hydrophobic sides towards the fat and hydrophilic towards the outside. The hydrophilic sides are positively charged due to the lecithin and other phospholipids that compose bile, and this charge prevents fat droplets coated with bile from re-aggregating into larger fat particles. Ordinarily, the micelles in the duodenum have a diameter of around 14-33 μm.
The dispersion of food fat into micelles thus provide a largely increased surface area for the action of the enzyme pancreatic lipase, which actually digests the triglycerides, and is able to reach the fatty core through gaps between the bile salts. A triglyceride is broken down into two fatty acids and a monoglyceride, which are absorbed by the villi on the intestine walls. After being transferred across the intestinal membrane, fatty acids are reformed into triglycerides, then absorbed into the lymphatic system through lacteals. Without bile salts, most of the lipids in the food would be passed out in feces, undigested.
Since bile increases the absorption of fats, it is an important part of the absorption of the fat-soluble substances, such as the vitamins D, E, K and A.
Besides its digestive function, bile serves also as the route of excretion for bilirubin, a byproduct of red blood cells recycled by the liver. Bilirubin derives from haemoglobin by glucuronidation.
The alkaline bile also has the function of neutralizing any excess stomach acid before it enters the ileum, the final section of the small intestine. Bile salts also act as bactericides, destroying many of the microbes that may be present in the food.
|CLICK IMAGE TO ENLARGE VIEW: source; http://bio1152.nicerweb.net/Locked/media/ch41/|
The Effects of Temperature Changes Salivary Amylase Activity
123HelpMe: the Effect of Temperature on Enzymes