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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 is a digestive enzyme that is predominantly secreted by the acinar cells of the exocrine pancreas.
Amylase is also secreted by the salivary glands. Pancreatic amylase is encoded by AMY2, and salivary amylase by AMY1, both genes on chromosome.
The main function of the amylases is to initiate the digestion of complex polysaccharides, primarily starch, to their constituent simple sugars.
This starts in the mouth with salivary α-amylase, which continues to work in the stomach (it is chemically protected from the gastric acid).
In the small bowel, starting in the duodenum, pancreatic amylase digests the dietary carbohydrate, aided by remnant salivary α-amylase.
Starch is mainly composed of two glucose polymers: amylopectin (75%) and amylose (25%), and the main action of amylase is to break their internal α1,4 linkages.
This results in the formation of oligosaccharides, which are primarily maltose, maltotriose, and α-limit dextrins
Amylase is found in small bowel intraluminal fluid and therefore bowel stasis can lead to abnormal absorption of the enzyme.
Amylases are enzymes that break starch down to sugar molecules.
Amylase is the major form of amylase found in humans and other mammals as well as an enzyme present in seeds, or in fungi (baker's yeast for instance).
Amylase is a calcium metalloenzyme, completely unable to function in the absence of calcium.
In human physiology, both the salivary and pancreatic amylases are major digestive enzymes.
Amylase begins the process of starch digestion.
Amylase takes starch chains and breaks them into smaller pieces with two or three glucose units.
Two similar types of amylase are made in your body--one is secreted in saliva, where it starts to break down starch grains as you chew, and the other is secreted by the pancreas, where it finishes its job.
Then, these little pieces are broken into individual glucose units by a collection of enzymes that are tethered to the walls of the intestine.
Since amylase needs to perform its job in the unpleasant environment of the intestine, it is a small, stable enzyme resistant to unfavorable conditions.
The amylase shown here (PDB entry 1ppi ) is made by the pancreas in pigs.
A small chain of five sugars (colored yellow) is bound in the active site, which is found in a large cleft on the enzyme.
Structures for the two human enzymes (which look very similar) are available in PDB entries.
As you look through the PDB, you will also find many structures of Amylases and other starch-digesting enzymes from bacteria and plants.
Amylases (1,4-α-D-glucan-4-glucanohydrolase, EC 3.2.1.1) are endoamylases catalyzing the hydrolysis of α- (1→4) glucosidic linkages of polysaccharides such as starch, glycogen etc.
In general they belong to class-13 of glycosyl hydrolases.
Amylases have the major world market share of enzymes.
These endoamylases are one of the most important enzymes for industrial and biotechnological applications.
Amylase holds key application in detergent, food, textile, pharmaceuticals, and bakery industries.
In this review, we summarize some important features, mechanism and physicochemical properties of amylase family.
In addition, applications and future prospects of industrially important enzyme having potential for biotechnological applications are discussed in detail.
Amylase is an enzyme found in bacteria and animal tissues that catalyzes the hydrolytic cleavage of starch and glycogen.
Serum amylase activity determinations are of clinical interest in the diagnosis of pancreatic function.
The enzymatic procedure presented is based on modifications of Wallenfels, using as substrate p-Nitrophenyl-D-maltoheptaoside (PNPG7) with the terminal glucose blocked to reduce spontaneous degradation of the substrate by glucosidase and glycoamylase.
The test is performed in a kinetic mode with a very short lag time and offers much greater stability than previous amylase methodologies.
Amylase hydrolyzes p-Nitrophenyl D-maltoheptaoside (PNPG7) to p-Nitrophenyl-maltotriose (PNPG3) and maltotetraose.
Glucoamylase hydrolyzes PNPG3 to p-Nitrophenylglycoside (PNPG1) and glucose.
Then PNPG1 is hydrolyzed by glucosidase to glucose and p-Nitrophenol, which produces a yellow color.
The rate of increase in absorbance is measured at 405 nm and is proportional to the amylase activity in the sample.
Amylases, which belong to glycoside hydrolase family 13, are 1,4-alpha-D-glucan glucanohydrolases, which degrade both the branched and unbranched forms of starch by cleaving the internal alpha-1,4 bonds connecting the glucose monomers.
The products of these reactions are maltose and maltotriose, which are further degraded to glucose by maltases.
One atom of calcium is required to bind to each protein molecule to allow it to function, but excess calcium can inhibit activity by binding to amino acids that are required for the catalytic activity of the enzyme.
Alpha Amylase is a major mash enzyme of critical concern to brewers in their production of fermentable wort.
Amylase digests starch, a large polymer of glucose, into smaller units, exposing it to further digestion by beta amylase.
Together these two amylases produce the spectrum of wort sugars essential in the production of a beer.
Amylase is an endo enzyme mainly digesting the alpha 1–4 bonds of starch at points within the chain, not at the ends.
Amylases are important hydrolase enzymes which have been widely used since many decades.
These enzymes randomly cleave internal glycosidic linkages in starch molecules to hydrolyze them and yield dextrins and oligosaccharides.
Among amylases α-Amylase is in maximum demand due to its wide range of applications in the industrial front.
Amylase can be produced by plant or microbial sources.
The ubiquitous nature, ease of production and broad spectrum of applications make amylase an industrially important enzyme.
To focus on the use of amylase in brewing, Amylase is necessary to look at the needs of a successful mash, in particular the spectrum of sugars required in the final wort.
Ideally these should be a suitable balance of simple fermentable sugars—glucose, maltose, and maltotriose—and larger unfermentable dextrins roughly in a 3:1 proportion.
Unlike wine, where virtually all of the sugars are fermented, beer is distinct in having residual sugars to provide sweetness, body, and mouthfeel.
Dextrins contribute strongly to this and give beer a major part of its character.
A starch molecule is, in essence, a group of glucose molecules linked together.
Enzymes break those links. Alpha amylase contributes to the digestion of starch by breaking internal bonds between glucose molecules.
As a result Amylase opens up the starch molecule, breaking it into a range of intermediate sizes.
Beta amylase further digests these intermediate molecules mostly into maltose—a sugar of two glucose units—but also to glucose itself and to the three-glucose molecule maltotriose.
The major limitation to this digestion is the side bonds of starch amylopectin, which are not digested by either alpha or beta amylase.
The parts of the starch molecule containing these side bonds form the basis of the important unfermentable dextrins produced by mashing.
The alpha amylase used in the mash comes from the malt, where it is entirely produced in the aleurone layer during malting.
In the barley seed, its mobilization is induced in order to digest the starch reserves in the endosperm and provide nutrients for the growing seed.
The maltster stops this at the point when enzyme levels are maximal and are preserved in the dry grain ready for use in mashing.
Levels of alpha amylase are typically high in pale malt but are virtually zero in roasted malt due to heat degradation.
Levels vary according to malt variety and to malting conditions.
Generally six-row barleys have higher levels than two-row barleys due to grains being smaller with less endosperm in proportion to aleurone.
Amylase is not restricted to barley but occurs in most organisms from bacteria to humans.
Salivary amylase, ptyalin, is a well-known amylase that initiates starch digestion in the mouth of mammals.
Enzymes tend to have specific temperature and pH ranges at which they will be active—this range is referred to as “optima.”
Amylase has a significantly different temperature and pH optima than beta amylase.
For amylase the temperature optima is higher at around 70°C compared to 60°C–65°C for beta amylase as the enzyme may be stabilized by calcium ions.
The pH optima of alpha amylase is also higher at 5.3–5.7 compared to 5.1–5.3 for beta amylase.
These differences can result in different wort sugar profiles from mashes conducted at different temperatures and are one means of varying beer character by control of mash conditions.
In traditional breweries, all the enzymes needed for brewing are contained within the natural ingredients out of which the beer is made.
However, exogenous alpha amylase is available in purified form from enzyme suppliers and may have different properties according to its origin.
These are widely used in the production of “light beers.”
The most relevant differences for brewers are thermal and pH tolerances.
Heat-labile alpha amylases can be used to supplement malt enzymes or to digest adjunct starch.
Because of their heat sensitivity, they will be denatured by pasteurization.
Heat-tolerant alpha amylases will, however, survive into the final beer, which may become sweeter over time if residual dextrins are available for digestion into flavor-active sugars.
Commercial alpha amylases may also cause problems if they are impure and contain beta amylase and proteases or if they contain toxins from their bacterial or fungal growth.
However, their use is growing in many food industries and will continue to have application in brewing, particularly if novel ingredients are sourced for future beers.
Amylase is the name given to glycoside hydrolase enzymes that break down starch into maltose molecules.
Although the amylases are designated by different Greek letters, they all act on α-1,4-glycosidic bonds.
Under the original name of diastase, amylase was the first enzyme to be found and isolated (by Anselme Payen in 1833).
Amylase is manufactured by fermentation of a microorganism that is not present in the final product.
Amylase catalyses the hydrolysis of starch into sugars and works great at breaking down starches.
This makes amylase a versatile ingredient that can used with the Spinzall and also in various baking applications.
The usage ratio for Amylase in baking is 0.01-0.05% bakers percentage.
Amylase (diastase) is supplied as a cream to white powder.
Amylase is a form of Amylase that acts on starch (amylose and amylopectin) and breaks it down to simple sugars such as maltose and dextrins.
Many organisms, including humans, use amylase to render dietary starch soluble so it can be absorbed during digestion.
Amylase (diastase) powder has undetectable levels (with Benedict's solution) of reducing sugars at a 0.5% solution (w/v), so the progress of the reaction can be monitored in two ways.
First, by using the iodine test to check for loss of the starch substrate.
Second, by using Benedict's solution to check for the appearance of reaction product (sugars).
Amylase, any member of a category of enzymes that catalyse the chemical reaction (splitting of a compound by addition of a water molecule) of starch into smaller saccharide molecules like maltose (a molecule composed of two glucose molecules).
Two classes of amylases, denoted alpha and beta, dissent within the method they attack the bonds of the starch molecules.
Amylase is widespread among living organisms.
The use of α-amylase in starch-based industries has been prevalent for many decades and a number of microbial sources exist for the efficient production of this enzyme, but only a few chosen strains of fungi and bacterium meet the factors for business production.
The search for new microorganisms that can be used for amylase production is a continuous process.
More recently, several authors have given sensible leads to developing α-amylase purification techniques, that modify applications in pharmaceutical and clinical sectors that need high purity amylases.
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 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.
USES:
FERMENTATION:
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.
FLOUR ADDITIVE:
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.
MOLECULAR BIOLOGY:
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.
USES:
Amylase enzymes are used extensively in bread making 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 into bread improver thereby making the bread making process faster and more practical for commercial use.
INDUSTRIAL USES:
Amylase is used in large quantities in the production of high fructose corn syrup, a mixture of sugars created from corn that is similar in taste and sweetness to the sucrose obtained from sugar beets and sugar cane.
The process requires three steps, each performed by a different enzyme.
Amylase performs the first step of breaking starch into small pieces.
Bacterial amylases, like the one shown on the left from PDB entry 2taa , are typically used since they are easy to obtain in large quantities.
The second step is performed by a fungal glucoamylase, shown here in the center from PDB entry 1dog.
It breaks the small chains into individual glucose units.
Unfortunately, glucose does not have a particularly palatable taste, so a third step must be added.
This is performed by glucose isomerase, also known as xylose isomerase, as shown on the right from PDB entry 4xia.
This enzyme converts some of the glucose into fructose, creating a tasty mixture that is used to sweeten everything from soft drinks to power bars.
However, this cheap and widely available sweetener may come with some disadvantages: a quick search on the WWW will reveal a whirlwind of controversy about the role of high fructose corn syrup in obesity and diabetes.
The active site of Amylase contains a trio of acidic groups (colored white and red) that do most of the work.
In the amylase shown here (PDB entry 1ppi ), glutamate 233, aspartate 197, and aspartate 300 work together to cleave the connection between two sugars in a starch
Amylase contains a short chain of five sugar units (colored yellow and orange) bound in the active site. The site of cleavage is shown in blue.
A calcium ion, shown as the large red sphere in the background, is found nearby where it stabilizes the structure of the enzyme.
A chloride ion, shown as a green sphere, is bound underneath the active site in many amylases, where it may assist the reaction.
The most widespread applications of alpha amylases are in the starch industry, which is used for starch hydrolysis in the starch liquefaction process that converts starch into fructose and glucose syrups.
The supermolecule conversion of all starch includes gelatinization, that involves the dissolution of starch granules, thereby forming a viscous suspension; phase change, that involves partial chemical reaction and loss in the body; and saccharification, involving the assembly of aldohexose and disaccharide via any reaction.
Initially, the alpha amylase of eubacteria amyloliquefaciens was used however it’s been replaced by the alpha amylase enzyme of eubacteria stearothermophilus or eubacteria licheniformis.
The enzymes from the eubacteria species are of interest group for large-scale biotechnological processes because of their exceptional thermostability and since economical expression systems are offered for these enzymes.
USES FOR DETERGENT INDUSTRY:
Detergent industries are the first customers of enzymes, in terms of each volume and price.
The use of enzymes in detergents formulations enhances the detergents ability to get rid of robust stains and creating the detergent environmentally safe.
Amylases are the second style of enzymes employed in the formulation of protein detergent, and ninetieth of all liquid detergents contain these enzymes.
These enzymes are utilised in detergents for laundry and automatic lavation to degrade the residues of starchy foods like potatoes, gravies, custard, chocolate, etc. to dextrins and alternative smaller oligosaccharides.
Amylases have activity at lower temperatures and base-forming pH scale, maintaining the required stability below detergent conditions and therefore the aerophilous stability of amylases is one among the foremost vital criteria for their use in detergents wherever the laundry surroundings are incredibly oxidising.
Removal of starch from surfaces is also important in providing a whiteness benefit since starch can be an attractant for many types of particulate soils.
Examples of amylases employed in the detergent business are derived from eubacteria or Aspergillus.
USES FOR FOOD INDUSTRY:
Amylases are extensively utilised in processed-food business like baking, brewing, preparation of digestive aids, production of cakes, fruit juices and starch syrups.
The amylases are wide employed in the baking business.
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.
Moreover, Amylase generates extra sugar within the dough, which improves the taste, crust colour and toasting qualities of the bread.
Besides generating possible compounds, α-amylases also have an anti-staling effect in bread baking, and they improve the softness retention of baked goods, increasing the shelf life of these products.
Currently, a thermostable maltogenic enzyme of eubacteria stearothermophilus is employed commercially within the bakehouse business.
Amylases are also used for the clarification of beer or fruit juices, or for the pre-treatment of animal feed to improve the digestibility of fibre.
USES FOR TEXTILE INDUSTRY:
Amylases are used in the textile industry for the de-sizing process.
Sizing agents like starch are applied to yarn before material production to make sure a quick and secure weaving method.
Amylase is a very attractive size, because Amylase is cheap, easily available in most regions of the world, and it can be removed quite easily.
Amylase is later far from the woven material in an exceedingly wet-process within the textile finishing business.
Amylase involves the removal of starch from the material that is the strengthening agent to forestall breaking of the warp thread throughout the weaving method.
The amylases take away by selection the dimensions and don’t attack the fibres.
Amylase from true bacteria stain was utilised in textile industries for quite a very long time.
USES FOR PAPER INDUSTRY:
The use of amylases within the pulp and paper business is for the modification of starch of coated paper, i.e. for the assembly of low-viscosity, high molecular weight starch.
The coating treatment serves to make the surface of paper sufficiently smooth and strong, to improve the writing quality of the paper.
During this application, the consistency of the natural starch is just very high for paper size and this may be altered by part degrading the chemical compound with α-amylases during a batch or continuous processes.
Amylase could be a sensible filler agent for the finishing of paper, improving the quality and erasability, besides being a good coating for the paper.
The size enhances the stiffness and strength in the paper.
MEDICAL USES:
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.
INDSUTRIAL USES:
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.
OTHER USES:
An inhibitor of 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.
BENEFITS:
Amylase’s primary function is digestion, but it may play a role in other facets of health as well, perhaps not directly, but as an indicator.
One study showed that people with metabolic syndrome are more likely to have low serum amylase levels.
Another study showed that levels of salivary Amylase were extremely sensitive to psychosocial stress.
This means that amylase may have future use as a means to help measure stress levels.
Amylase has one additional small but important role – processing and digesting dead white blood cells.
There are several potential issues that can lead to enzyme deficiencies or imbalances.
Some of the most common are issues with the pancreas, but alcoholism and certain medications can impact the levels of amylase that you have in your body.
Also, we naturally start producing lower levels of amylase as we age.
If you find that eating starchy foods is giving you inordinate amounts of discomfort, it would be worthwhile to meet with your doctor and have your amylase levels checked.
If digestive enzymes are found to be low or suspected to be low, supplementation can be an ideal way to increase your digestive enzyme levels and lead to better digestive health overall.
Amylase’s primary function is digestion, but it may play a role in other facets of health as well, perhaps not directly, but as an indicator. One study showed that people with metabolic syndrome are more likely to have low serum amylase levels.
Another study showed that levels of salivary Amylase were extremely sensitive to psychosocial stress.
This means that amylase may have future use as a means to help measure stress levels.
Amylase has one additional small but important role processing and digesting dead white blood cells.
Amylase is an important part of your digestive health, but the best way to get the most out of it is to combine it with other factors in order to get the maximum effect.
One way to do this is through supplements like Enzymedica’s Chewable Digest.
Naturally orange flavored and sweetened with sugar-free Xylitol, this contains amylase, lipase, cellulase and protease Thera-blend™ enzymes, which help you digest a variety of different foods.
Thera-blend combines several strains of enzymes to get stronger and faster results.
There are a number of potential issues that can lead to enzyme deficiencies or imbalances.
Some of the most common are issues with the pancreas, but alcoholism and certain medications can impact the levels of amylase that you have in your body.
Also, we naturally start producing lower levels of amylase as we age.
If you find that eating starchy foods is giving you inordinate amounts of discomfort, it would be worthwhile to meet with your doctor and have your amylase levels checked. Being cautious now can save you from larger issues later.
FUNCTION:
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.
