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CAS NUMBER: 9014-71-5

EC / LIST NUMBER: 618-485-8

Amylase is an enzyme that catalyses the hydrolysis of starch (Latin amylum) into sugars. 
Amylase is present in the saliva of humans and some other mammals, where it begins the chemical process of digestion. 
Foods that contain large amounts of starch but little sugar, such as rice and potatoes, may acquire a slightly sweet taste as they are chewed because amylase degrades some of their starch into sugar. 

The pancreas and salivary gland make 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. 
Specific amylase proteins are designated by different Greek letters. 

All amylases are glycoside hydrolases and act on α-1,4-glycosidic bonds.
Amylase is a digestive enzyme predominantly secreted by the pancreas and salivary glands and found in other tissues in very small levels. 
Amylase was first described in the early 1800s and is considered one of the first enzymes in history to be scientifically investigated. 

Amylase was initially termed as diastaste but was later renamed amylase in the early 20th century.
Amylase is an enzyme that catalyzes the hydrolysis of internal α-1,4-glycosidic linkages in starch and glycogen, yielding such glucose, maltose and maltotriose units. 

Amylase is the major form of amylase found in humans and other mammals. 
Amylase is also secreted by many fungi, and present in seeds containing starch as a food reserve. 
Amylases are among the most important enzymes and are of great significance for biotechnology, constituting a class of industrial enzymes having approximately 25% of the world enzyme market, which have potential application in a wide number of industrial processes such as food, fermentation, textile, paper, detergent, and pharmaceutical industries.

Amylases are widespread in animals, fungi, plants, and are also found in the unicellular eukaryotes, bacteria and archaea. 
Ptyalin, a salivary α-amylase (α-1,4-α-D-glucan-4-glucanohydrolase) is one of the most important enzymes in saliva. 
Fungal sources of α-Amylase are confined to terrestrial isolates, mostly to Aspergillus species and to only few species of Penicillium, P. brunneum being one of them. 

The fungal source used predominantly for commercial production of α-Amylase are the strains of Aspergillus spp. Aspergillus oryzae, A. niger and A. awamori are most commonly used species for commercial production among several others. 
Amylase can be produced by different species of bacteria, but for commercial applications α-amylase is mainly derived from the genus Bacillus. 

Amylases produced from Bacillus licheniformis, Bacillus stearothermophilus, and Bacillus amyloliquefaciens find potential application in a number of industrial processes such as in food, fermentation, textiles and paper industries. 
Plant sources had not been considered with enough significance as the source of these enzymes yet. 

Amylase in protein structure ensures that the elements taken into the body with food are digested and broken down in the small intestines. 
Amylase, which is responsible for the digestion of carbohydrates, is contained in the secretions of the pancreas, which acts as a gland, and is released into the small intestine. 
Small amounts are also found in the small intestine, placenta, and ovaries.

Amylase is a digestive enzyme that breaks down carbohydrates into smaller pieces. 
In addition to the enzyme amylase, which is secreted by production in the pancreas, another form, alpha amylase, is also secreted from the salivary glands. 

With the blood test performed in this direction, Amylase is understood whether the amylase enzyme is in the reference range. 
Accordingly, possible problems that may occur in the pancreas can be understood by its lowness or height.
Generally, the amylase enzyme can be detected with both a blood test and a urine test. 

However, to obtain more precise results, hemoglobin is added to the reference range and a comparison is made with the blood count. 
There are many different factors that affect the level of amylase. 
In the face of possible problems, diagnosis and analysis are performed together with blood tests for the pancreas.


Amylases' main function is to hydrolyze the glycosidic bonds in starch molecules, converting complex carbohydrates to simple sugars. 
There are three main classes of amylase enzymes; Alpha-, beta- and gamma-amylase, and each act on different parts of the carbohydrate molecule. 
Amylase can be found in humans, animals, plants, and microbes. 

Amylase is found in microbes and plants. Gamma-amylase is found in animals and plants. 
This article will focus on alpha-amylase and its applications.
Amylase is a calcium dependent enzyme which hydrolyzes complex carbohydrates at alpha 1,4-linkages to form maltose and glucose. 

Amylase is filtered by renal tubules and resorbed (inactivated) by tubular epithelium. 
Active enzyme does not appear in urine. Small amounts of amylase are taken up by Kupffer cells in the liver. 
In healthy dogs, 14% of amylase is bound to globulins. Because of this polymerization, canine amylase has variable (high) molecular weights and is not normally filtered by the kidney. 

In dogs with renal disease, this polymerized (macroamylase) amylase is found in higher concentration (from 5-62% of total amylase activity) and contributes to the hyperamylasemia seen in these disorders.
The amylase enzymes are a group of hydrolases that degrade complex carbohydrates into fragments. 
Amylase is produced primarily by the exocrine pancreas where the enzyme is synthesized by the acinar cells and then secreted into the intestinal tract by way of the pancreatic duct system. 

Amylases also are produced by the salivary glands, small intestine mucosa, ovaries, placenta, liver, and fallopian tubes. Pancreatic and salivary isoenzymes are found in serum.
Amylase is widely distributed in nature. 

Amylase is present in both plants and animals. 
Cereal and grains and their flours naturally contain different types of amylase. 
In cereals, it is found in the endosperm, bran and germ.

In 1908, a study by Wohlgemuth identified the presence of amylase in urine, and this subsequently led to the use of amylase as a diagnostic laboratory test. 
Amylase is a commonly ordered test along with lipase, especially in the setting of suspected acute pancreatitis.
Amylases are a class of enzymes that catalyze the hydrolysis of starch into sugars such as glucose and maltose.



Amylases are important in brewing beer and liquor made from sugars derived from starch. 
In fermentation, yeast ingests sugars and excretes ethanol. 
In beer and some liquors, the sugars present at the beginning of fermentation have been produced by "mashing" grains or other starch sources (such as potatoes). 

In traditional beer brewing, malted barley is mixed with hot water to create a "mash", which is held at a given temperature to allow the amylases in the malted grain to convert the barley's starch into sugars. 
Different temperatures optimize the activity of alpha or beta amylase, resulting in different mixtures of fermentable and unfermentable sugars. 
In selecting mash temperature and grain-to-water ratio, a brewer can change the alcohol content, mouthfeel, aroma, and flavor of the finished beer.

In some historic methods of producing alcoholic beverages, the conversion of starch to sugar starts with the brewer chewing grain to mix it with saliva. 
This practice continues to be practiced in home production of some traditional drinks, such as chhaang in the Himalayas, chicha in the Andes and kasiri in Brazil and Suriname.


Amylases are used in breadmaking 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 ethanol and carbon dioxide. 
This imparts flavour and causes the bread to rise. 
While amylases are found naturally in yeast cells, Amylase 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 sourdough. 
Modern breadmaking techniques have included amylases (often in the form of malted barley) into bread improver, thereby making the process faster and more practical for commercial use.
Amylase is often listed as an ingredient on commercially package-milled flour. Bakers with long exposure to amylase-enriched flour are at risk of developing dermatitis or asthma.


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.


Amylase also has medical applications in the use of pancreatic enzyme replacement therapy (PERT). 
Amylase is one of the components in Sollpura (liprotamase) to help in the breakdown of saccharides into simple sugars.


Amylase is used extensively in various industrial processes. 
In textile weaving, starch is added for warping. 
After weaving, the starch is removed by Bacillus subtilis α-amylase. 
Dextrin, which is a viscosity improver, filler, or ingredient of food, is manufactured by the liquefaction of starch by bacteria α-amylase. 
Bacterial α-amylases of B.subtilis, or B.licheniformis are used for the initial starch liquefaction in producing high conversion glucose syrup. 
Pancreatitis can be tested by determining the level of amylases in the blood, a result of damaged amylase-producing cells, or excretion due to renal failure. 

Amylase is used for the production of malt, as the enzyme is produced during the germination of cereal grains. 
Amylase is a precursor protein which is cleaved to form the β-amylase and α-amylase after secretion.
The most widespread applications of α-amylases are in the starch industry, which are used for starch hydrolysis in the starch liquefaction process that converts starch into fructose and glucose syrups. 

The use of enzymes in detergents formulations enhances the detergents ability to remove tough stains and making the detergent environmentally safe. 
Amylases are the second type of enzymes used in the formulation of enzymatic detergent, and 90% of all liquid detergents contain these enzymes. 

Textile industries are extensively using alpha amylases to hydrolyze and solubilize the starch, which then wash out of the cloth for increasing the stiffness of the finished products. 
More than 70% bread in U.S.A, Russia and European countries contain alpha amylase. 

Amylases play important role in bakery products. 
These enzymes can be added to the dough of bread to degrade the starch in the flour into smaller dextrins, which are subsequently fermented by the yeast. 
The addition of α-amylase to the dough results in enhancing the rate of fermentation and the reduction of the viscosity of dough, resulting in improvements in the volume and texture of the product.


An inhibitor of alpha-amylase, called phaseolamin, has been tested as a potential diet aid.
Amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. 
Amylase, has been used in various plant studies, such as carbon starvation studies in Populus tremuloides. 
Amylase, from barley, has been used to study how pressure and temperature affect catalytic activity.

Amylase is a gel filtration molecular weight marker that can be used in gel filtration chromatography and protein chromatography. 
When used as a food additive, amylase has E number E1100, and may be derived from pig pancreas or mold fungi.
Bacilliary amylase is also used in clothing and dishwasher detergents to dissolve starches from fabrics and dishes.
Factory workers who work with amylase for any of the above uses are at increased risk of occupational asthma. 
Five to nine percent of bakers have a positive skin test, and a fourth to a third of bakers with breathing problems are hypersensitive to amylase.


In the human body, Amylase is part of digestion with the breakdown of carbohydrates in the diet. 
The mechanism involved includes catalyzing substrate hydrolysis by a double replacement mechanism, forming a covalent glycosyl-enzyme intermediate and hydrolyzed through oxocarbenium ion-like transition states. 

One of the carboxylic acids in the active site acts as the catalytic nucleophile during the formation of the intermediate. 
A second carboxylic acid operates as the acid/base catalyst, supporting the stabilization of the transition states during the hydrolysis.
Amylases perform the following functions in bakery products:

-Provide fermentable and reducing sugars.
-Accelerate yeast fermentation and boost gassing for optimum dough expansion during proofing and baking
-Intensify flavors and crust color by enhancing Maillard browning and caramelization reactions.
-Reduce dough/batter viscosity during starch gelatinization in the oven.
-Extend oven rise/spring and improve product volume.
-Act as crumb softeners by inhibiting staling.
-Modify dough handling properties by reducing stickiness.

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