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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.
CAS: 9000-90-2
EINECS: 232-565-6
Synonyms
ALPHA-AMYLASE, TYPE X1-A;ALPHA-AMYLASE TYPE XII-A;ALPHA-AMYLASE TYPE XIII-A;3.2.1.1;1,4-ALPHA-D-GLUCAN-GLUCANOHYDROLASE TYPE XII-A;1,4-ALPHA-D-GLUCAN-GLUCANOHYDROLASE TYPE XIII-A;1,4-ALPHA-D-GLUCAN-GLUCANOHYDROLASE;1,4-ALPHA-D-GLUCAN-GLUCANOHYDROLASE TYPE I-A
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 kind of enzyme being able to hydrolyzes alpha bonds of large alpha-linked polysaccharides including starch and glycogen.
Amylase is a very small, stable enzyme which is resistant to many unfavorable conditions.
Amylase can hydrolyzes starch and glycogen to maltose and glucose, respectively so that providing energy for human beings and animals.
Amylase is present in almost all kinds of plants, animals and microbes.
Amylase has many industrial applications.
For example, Amylase can be used in the production of ethanol through breaking starches in grains into fermentable sugars.
Amylase can also be used during the production of high-fructose corn syrup.
In addition, Amylase can be used in some dishwashing and starch-removing detergents.
Amylase has been enhanced for energy efficiency and waste prevention when used in starch ethanol research.
Amylase is an enzyme that catalyzes the hydrolysis of starch into sugars, playing a crucial role in carbohydrate digestion.
Amylase is classified as an endoamylase, meaning it acts on the internal bonds of the starch molecule, breaking it down into smaller oligosaccharides and eventually into glucose.
Amylase is produced by various organisms, including plants, bacteria, and fungi, and is particularly abundant in saliva and pancreatic secretions in humans.
Amylase operates optimally at a specific pH and temperature, which can vary depending on its source.
Amylase is widely used in various industries, including food processing, brewing, and pharmaceuticals, due to its ability to enhance the sweetness and digestibility of starches.
Additionally, Amylase is important in clinical diagnostics, as its levels can indicate certain health conditions, such as pancreatitis.
The enzyme is characterized by its glycosyl hydrolase activity and is often studied for its structural and functional properties, which are essential for understanding its mechanism of action and potential applications.
Amylase Chemical Properties
Melting point: 66-73 °C
density: 1.37[at 20℃]
vapor pressure: 0Pa at 25℃
storage temp.: -20°C
solubility: H2O: soluble0.1mg/mL, clear, colorless
form: suspension
color: yellow-brown
biological source: human pancreas
Water Solubility: 100g/L at 25℃
Merck: 14,599
Specific Activity: 300-1,500units/mg protein
LogP: -1.3 at 20℃
EPA Substance Registry System: Amylase(9000-90-2)
Nearly white to light brownish yellow amorphous powder, or light brownish yellow to dark brown liquid.
Almost insoluble in ethanol, chloroform and ether.
Soluble in water, the aqueous solution is pale yellow to dark brown.
Uses
Amylase from Bacillus sp. has been used:
as a dispersal enzyme to test degradation ofS. aureusbiofilms,
in the enzymatic hydrolysis of tapioca starch
in the enzymolysisof plant-based native and the amorphous granular starches
Amylase has been used in various plant studies, such as metabolism studies in Arabidopsis.
Amylase from human pancreas has been used to test interference for enzymatic methods of assaying calcium in serum and urine.
Amylase, from Sigma, has been used to get a standard calibration curve during the evaluation of an automated amylase detection system using forensic samples.
Amylase is to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. Product A1031 is from human saliva, is type IIA, and is supplied as a lyophilized powder.
Amylase has been used in various plant studies, such as metabolism studies in Arabidopsis 1 .
Amylase from human saliva has been used to study the development of nutraceuticals, which may aid the treatment of diabetes and obesity.
Fermentation
α- and β-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, it takes time for the yeast to produce enough of these enzymes to break down significant quantities of starch in the bread.
Amylase 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.
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.
Scientific uses
Salivary alpha-amylase serves as a biomarker for physiological stress.
In response to sympathetic nervous system activity (for example due to a real-life stressor), the level of Amylase in the saliva is known to increase; therefore, the amount of alpha-amylase in the saliva can inform researchers specifically about the sympathetic nervous system activity component of the stress response.
Like with other biomarkers for stress, Amylase is known that the salivary alpha-amylase response to stress is reduced in intensity in people with occupational burnout.
Other uses
An inhibitor of Amylase, called phaseolamin, has been tested as a potential diet aid.
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.
Biotechnological Production
Amylase degrade starch and similar carbohydrates by endohydrolysis of their (1→4)-a-D-glucosidic bonds.
The majority of a-amylases belong to the group of metalloenzymes and require calcium ions (Ca2+).
By means of direct evolution, the performance of several amylases was further maximized and adapted to the needs of the starch processing industry.
The enhancement of the thermostability of amylase was achieved by DNA-shuffling techniques.
The baking industry and consumers might benefit from genetically optimized starch-modifying enzymes.
Based on the improved thermal stability of an a-amylase in the acidic pH range, the retrogradation of sourdough breads ("staling") can be delayed.
Biochem/physiol Actions
Amylase catalyses the hydrolysis of α-1,4 glycosidic linkage in oligosaccharides.
Amylase plays a crucial role in the initial digestion of starch, glycogen and polysaccharides.
Elevated levels of amylase in serum is linked to acute pancreatitis.
