AMYLASE

Amylase is combined with alkalies as an antacid in Takazyme,with vitamins in Taka-Combex, and in other preparations.
Amylase of the controlled germination of barley. 
Amylase presents as a clear amber to dark brown liquid or white to tan powder.

CAS Number: 9000-92-4
EINECS Number: 232-567-7

Synonyms: CHEMBL65761, 148404-10-8, alpha-Amylase-IN-1, BDBM50292167, TS-09303, 1-[3-(4-Hydroxy-phenyl)-5-(4-methoxy-phenyl)-4,5-dihydro-pyrazol-1-yl]-ethanone, 1-[3-(4-hydroxyphenyl)-5-(4-methoxyphenyl)-4,5-dihydro-1H-pyrazol-1-yl]ethan-1-oneMALTIN,MALT DIASTASE, MALT, DIASTASE, DIASTASE (ASPERGILLUS ORYZAE), DIASTASE (EX MALT), DIASTASE (MALT), DIASTASE OF MALT

Amylase is derived from theaction of a fungus, Aspergillus oryzae Cohn (Ahlburg), on ricehulls or wheat bran. 
Amylase is a yellow, hygroscopic, almost tastelesspowder that is freely soluble in water and can solubilize300 times its weight of starch in 10 minutes. 
Amylase is used in dosesof 0.3 to 1.0 g in the same conditions as malt diastase. 

A class of enzymes which convert starch into sugars. 
Fungal and bacterial Amylase from specific fungi and bacteria have been suggested for commercial fermentation processes.
Amylase is an enzyme that hydrolyzes starch. 

These enzymes, widely distributed in animals and plants, break down starch or glycogen to dextrin, maltose or glucose. 
Amylase in human saliva is called ptyalin.
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 class of enzymes that plays a crucial role in the breakdown of carbohydrates, specifically polysaccharides like starch and glycogen, into simpler sugars such as maltose and glucose. 
These enzymes are essential for various biological and industrial processes, as they catalyze the hydrolysis of glycosidic bonds in carbohydrate molecules. 
Found in almost all living organisms, amylase is critical to the digestion and energy metabolism processes of plants, animals, and microorganisms.

In humans and other animals, amylase is predominantly produced in the salivary glands and the pancreas. 
Salivary amylase, also known as ptyalin, initiates the digestion of starches in the mouth, breaking them down into smaller carbohydrate chains as part of the first step of the digestive process. 
This enzymatic activity continues briefly in the stomach until the acidic environment inhibits the enzyme's function. 

Pancreatic Amylase, on the other hand, is secreted into the small intestine, where it further degrades partially digested starches into maltose and other disaccharides. 
These simpler sugars are eventually converted into glucose, which the body absorbs and utilizes as a primary energy source.
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.
Amylases are a food source rich in energy. 
Large polymers such as starch are partially hydrolyzed in the mouth by the enzyme amylase before being cleaved further into sugars. 

Many mammals have seen great expansions in the copy number of the amylase gene. 
These duplications allow for the pancreatic amylase AMY2 to re-target to the salivary glands, allowing animals to detect starch by taste and to digest starch more efficiently and in higher quantities. 
This has happened independently in mice, rats, dogs, pigs, and most importantly, humans after the agricultural revolution.

Following the agricultural revolution 12,000 years ago, human diet began to shift more to plant and animal domestication in place of hunting and gathering. 
Starch has become a staple of the human diet.
Despite the obvious benefits, early humans did not possess salivary amylase, a trend that is also seen in evolutionary relatives of the human, such as chimpanzees and bonobos, who possess either one or no copies of the gene responsible for producing salivary amylase.

However, not all humans possess the same number of copies of the AMY1 gene. 
Populations known to rely more on saccharides have a higher number of AMY1 copies than human populations that, by comparison, consume little starch. 
The number of Amylase gene copies in humans can range from six copies in agricultural groups such as European-American and Japanese (two high starch populations) to only two to three copies in hunter-gatherer societies such as the Biaka, Datog, and Yakuts.

The correlation that exists between starch consumption and number of Amylase copies specific to population suggest that more AMY1 copies in high starch populations has been selected for by natural selection and considered the favorable phenotype for those individuals. 
Therefore, it is most likely that the benefit of an individual possessing more copies of AMY1 in a high starch population increases fitness and produces healthier, fitter offspring.

This fact is especially apparent when comparing geographically close populations with different eating habits that possess a different number of copies of the AMY1 gene. 
Such is the case for some Asian populations that have been shown to possess few AMY1 copies relative to some agricultural populations in Asia. 
This offers strong evidence that natural selection has acted on this gene as opposed to the possibility that the gene has spread through genetic drift.

Variations of amylase copy number in dogs mirrors that of human populations, suggesting they acquired the extra copies as they followed humans around.
Unlike humans whose amylase levels depend on starch content in diet, wild animals eating a broad range of foods tend to have more copies of amylase. 
This may have to do with mainly detection of starch as opposed to digestion.

Amylase, any member of a class of enzymes that catalyze the hydrolysis (splitting of a compound by addition of a water molecule) of starch into smaller carbohydrate molecules such as maltose (a molecule composed of two glucose molecules). 
Three categories of amylases, denoted alpha, beta, and gamma, differ in the way they attack the bonds of the starch molecules.
Alpha-amylase is widespread among living organisms. 

In the digestive systems of humans and many other mammals, an alpha-amylase called ptyalin is produced by the salivary glands, whereas pancreatic amylase is secreted by the pancreas into the small intestine. 
Amylase is mixed with food in the mouth, where it acts upon starches. Although the food remains in the mouth for only a short time, the action of ptyalin continues for up to several hours in the stomach—until the food is mixed with the stomach secretions, the high acidity of which inactivates ptyalin. 
Amylase’s digestive action depends upon how much acid is in the stomach, how rapidly the stomach contents empty, and how thoroughly the food has mixed with the acid. 

Under optimal conditions as much as 30 to 40 percent of ingested starches can be broken down to maltose by ptyalin during digestion in the stomach.
Amylase is an enzyme (EC 3.2.1.1; systematic name 4-α-D-glucan glucanohydrolase) that hydrolyses α bonds of large, α-linked polysaccharides, such as starch and glycogen, yielding shorter chains thereof, dextrins, and maltose, through the following biochemical process.

Amylase is the major form of amylase found in humans and other mammals.
Amylase is also present in seeds containing starch as a food reserve, and is secreted by many fungi. 
It is a member of glycoside hydrolase family 13.

Although found in many tissues, amylase is most prominent in pancreatic juice and saliva, each of which has its own isoform of human α-amylase. 
They behave differently on isoelectric focusing, and can also be separated in testing by using specific monoclonal antibodies. 
In humans, all amylase isoforms link to chromosome 1p21 (see AMY1A).

An amylase test measures the amount of amylase in blood or urine (pee). Amylase is an enzyme, a protein that speeds up chemical reactions in body. 
Amylase helps you digest carbohydrates. Most of the amylase in your body is made by pancreas and salivary (spit) glands.
Amylase's normal to have a small amount of amylase in your blood and urine. 

But having too much amylase may be a sign of a disorder of the pancreas or salivary glands or another medical condition.
Tests for amylase in blood or urine are mainly used to diagnose problems with your pancreas, including pancreatitis, which is inflammation of the pancreas. 
The test is also used to monitor chronic (long-term) pancreatitis.

Changes in amylase levels show up in blood before urine, so an amylase urine test may be done with or after an amylase blood test.
One or both types of amylase test may also be used to help diagnose or monitor treatment for other disorders that may affect amylase levels, such as salivary gland disorders and certain digestive conditions.
An amylase test is a way to measure the amount of amylase in blood or urine (pee).

Amylase’s also called an “amy” test, serum amylase and urine amylase.
Amylase is an enzyme, a type of protein that helps your body break down carbohydrates. 
The pancreas and salivary glands in your mouth make amylase.

There’s normally a small amount of amylase in your blood and urine. 
But levels that are too high can indicate a health problem.
There are different types of amylase, with the most common being α-amylase, β-amylase, and γ-amylase, each of which has specific roles and functions.

Amylase, found in humans and many other organisms, cleaves starch molecules randomly to produce smaller carbohydrate chains, making it an essential enzyme for efficient energy extraction. 
β-Amylase is more common in plants and microorganisms, and it works by cleaving starch from the non-reducing end to produce maltose. 
γ-Amylase, also known as glucoamylase, hydrolyzes starch into glucose by removing single glucose units from the ends of polysaccharide chains.

In industrial applications, amylase is an indispensable enzyme used in a wide range of processes. 
It is a key ingredient in the production of bread, beer, and other fermented products, where it helps break down starches in grains to release sugars that yeast ferments into alcohol and carbon dioxide. 
In the textile industry, amylase is used to remove starch-based sizing agents from fabrics, improving the texture and quality of the finished product. 

Additionally, amylase plays a vital role in the production of high-fructose corn syrup, where it helps convert corn starch into sugars that are further processed into sweeteners.
Amylase is also extensively used in the pharmaceutical and diagnostic fields. 
In medicine, it is included in certain digestive enzyme supplements to assist individuals with pancreatic insufficiency or other digestive disorders in breaking down starches more effectively.

In diagnostics, amylase levels in blood or urine are measured to detect and monitor conditions such as pancreatitis or other pancreatic disorders. 
Elevated or decreased levels of amylase can provide valuable information about the state of a person's digestive health and metabolic function.

storage temp.:    2-8°C
solubility: Sparingly soluble in water (except when admixed with an insoluble diluents ); insoluble in ethanol (95 per cent) and in ether
form: powder
color: white
Odor: Odorless
PH Range: 5.5 - 6.0
Merck: 599
Dielectric constant: 2.7（Ambient）
Stability: Stable. Incompatible with strong oxidizing agents.

Amylase is a highly specialized enzyme that plays a critical role in the breakdown of complex carbohydrates into simpler sugars. 
This process is fundamental not only for digestion and metabolism but also for numerous industrial applications, making amylase one of the most studied and widely used enzymes in both biological and commercial contexts.
Biologically, amylase is a part of a broader class of enzymes that catalyze the hydrolysis of starches and glycogen. 

These polysaccharides, which are large molecules made up of repeating glucose units, serve as storage forms of energy in plants and animals. 
Amylase accelerates the breakdown of these long chains into smaller sugars, which the body can then use for energy. 
Amylase operates by cleaving the glycosidic bonds between sugar units in the polysaccharide, transforming starch into maltose, glucose, and other oligosaccharides.

In humans, amylase is primarily produced in the salivary glands and pancreas. 
Salivary amylase, also known as ptyalin, begins the digestion of starches in the mouth. 
As food is chewed, salivary amylase acts on the starch in the food, breaking it into smaller molecules, which will continue to be processed in the stomach and small intestine. 

When the food reaches the stomach, the enzyme's activity diminishes due to the acidic environment, but in the small intestine, pancreatic amylase takes over to complete the breakdown of starch into sugars. 
This process helps the body absorb glucose, which is then transported through the bloodstream and used as a primary energy source for various physiological functions.
Amylase is essential not only in human digestion but also in other species. 

In plants, amylase plays a key role in seed germination. 
As seeds begin to sprout, amylase breaks down stored starch into sugars that provide the initial energy required for growth. 
In microorganisms, Amylase assists in the breakdown of starches to generate fermentable sugars, supporting metabolic processes that can produce a variety of end products, including alcohols, acids, and other chemicals.
There are various types of amylase enzymes, the most common being α-amylase, β-amylase, and γ-amylase. 

Each type of amylase works in slightly different ways. 
Amylase, found in humans, animals, and many bacteria, is the most important for starch digestion. 
It cleaves long starch molecules at random points along their structure, producing a mixture of oligosaccharides.

Amylase, commonly found in plants and fungi, works by cleaving two glucose units at a time from the non-reducing end of the starch molecule, resulting in maltose. 
Amylase, or glucoamylase, is involved in breaking down starch all the way to glucose units, which is especially important in processes that require complete breakdown of starch.
Amylase also has significant industrial applications due to its ability to degrade starch into fermentable sugars. 

In the food and beverage industry, amylase is widely used in the production of products like bread, beer, and various sweeteners. 
In bread-making, amylase helps convert starches in flour into sugars, which yeast then ferments to produce carbon dioxide, causing the dough to rise. 
In brewing, amylase breaks down the starch in barley and other grains into fermentable sugars, which yeast then ferments into alcohol. 

One of the key industrial applications of amylase is the production of high-fructose corn syrup (HFCS), where amylase is used to convert corn starch into sugars that are then processed into syrup used in many sweetened foods and drinks.
In the textile industry, amylase is used for desizing, which involves removing starch-based sizing agents from fabrics. 
These agents are often used during the weaving process to strengthen threads, but they must be removed before the fabric can be dyed or finished. 

Amylase is employed to break down these starches, improving the quality and texture of the fabric while ensuring that the dyeing process proceeds smoothly.
In the pharmaceutical industry, amylase is often used in enzyme supplements for individuals with pancreatic insufficiency or other digestive disorders. 
These supplements aid in the breakdown of starches and other carbohydrates, helping to alleviate symptoms of poor digestion and nutrient malabsorption. 

Furthermore, amylase is measured in clinical settings to diagnose and monitor conditions such as pancreatitis. 
Elevated levels of amylase in the blood or urine can indicate pancreatic damage, while abnormal levels can help doctors assess the severity of the disease.
Amylase’s importance extends into biotechnology and environmental applications as well. 

In biotechnology, engineered forms of amylase are used in processes such as the production of biofuels, where starch is fermented into ethanol. 
Additionally, amylase is utilized in the paper and pulp industries to improve paper quality by breaking down starch residues in the pulp. 
The enzyme is also explored for use in the bioremediation of polluted sites, where its ability to degrade starches can be harnessed to break down organic pollutants.

Amylase are calcium metalloenzymes. 
By acting at random locations along the starch chain, α-amylase breaks down long-chain saccharides, ultimately yielding either maltotriose and maltose from amylose, or maltose, glucose and "limit dextrin" from amylopectin. 
Because it can act anywhere on the substrate, α-amylase tends to be faster-acting than β-amylase. 

In animals, Amylase is a major digestive enzyme, and its optimum pH is 6.7–7.0.
In human physiology, both the salivary and pancreatic amylases are α-amylases.
The α-amylase form is also found in plants, fungi (ascomycetes and basidiomycetes) and bacteria (Bacillus).

Another form of amylase, β-amylase (EC 3.2.1.2 ) (alternative names: 1,4-α-D-glucan maltohydrolase; glycogenase; saccharogen amylase) is also synthesized by bacteria, fungi, and plants. 
Working from the non-reducing end, β-amylase catalyzes the hydrolysis of the second α-1,4 glycosidic bond, cleaving off two glucose units (maltose) at a time. 
During the ripening of fruit, β-amylase breaks starch into maltose, resulting in the sweet flavor of ripe fruit. 

They belong to glycoside hydrolase family 14.
Both α-amylase and β-amylase are present in seeds; β-amylase is present in an inactive form prior to germination, whereas α-amylase and proteases appear once germination has begun. 
Many microbes also produce amylase to degrade extracellular starches. 

Animal tissues do not contain β-amylase, although it may be present in microorganisms contained within the digestive tract. 
Blood serum amylase may be measured for purposes of medical diagnosis. 
A higher than normal concentration may reflect any of several medical conditions, including acute inflammation of the pancreas (which may be measured concurrently with the more specific lipase), perforated peptic ulcer, torsion of an ovarian cyst, strangulation, ileus, mesenteric ischemia, macroamylasemia and mumps. Amylase may be measured in other body fluids, including urine and peritoneal fluid.

A January 2007 study from Washington University in St. Louis suggests that saliva tests of the enzyme could be used to indicate sleep deficits, as the enzyme increases its activity in correlation with the length of time a subject has been deprived of sleep.
Amylase also has medical applications in the use of pancreatic enzyme replacement therapy (PERT). 
It is one of the components in Sollpura (liprotamase) to help in the breakdown of saccharides into simple sugars.

Amylase is found in saliva and breaks starch into maltose and dextrin. 
This form of amylase is also called "ptyalin" /ˈtaɪəlɪn/, which was named by chemist Jöns Jacob Berzelius. 
The name derives from the Greek word πτυω (I spit), because the substance was obtained from saliva.

Amylase will break large, insoluble starch molecules into soluble starches (amylodextrin, erythrodextrin, and achrodextrin) producing successively smaller starches and ultimately maltose. 
Ptyalin acts on linear α(1,4) glycosidic linkages, but compound hydrolysis requires an enzyme that acts on branched products. 
Salivary amylase is inactivated in the stomach by gastric acid. In gastric juice adjusted to pH 3.3, ptyalin was totally inactivated in 20 minutes at 37 °C. 

In contrast, 50% of amylase activity remained after 150 minutes of exposure to gastric juice at pH 4.3.
Both starch, the substrate for ptyalin, and the product (short chains of glucose) are able to partially protect it against inactivation by gastric acid. 
Amylase added to buffer at pH 3.0 underwent complete inactivation in 120 minutes; however, addition of starch at a 0.1% level resulted in 10% of the activity remaining, and similar addition of starch to a 1.0% level resulted in about 40% of the activity remaining at 120 minutes.

The salivary amylase gene has undergone duplication during evolution, and DNA hybridization studies indicate many individuals have multiple tandem repeats of the gene. 
The number of gene copies correlates with the levels of salivary amylase, as measured by protein blot assays using antibodies to human amylase. 
Gene copy number is associated with apparent evolutionary exposure to high-starch diets.

For example, a Japanese individual had 14 copies of the amylase gene (one allele with 10 copies, and a second allele with four copies). 
The Japanese diet has traditionally contained large amounts of rice starch. 
In contrast, a Biaka individual carried six copies (three copies on each allele). 

The Biaka are rainforest hunter-gatherers who have traditionally consumed a low-starch diet.
Perry and colleagues speculated the increased copy number of the salivary amylase gene may have enhanced survival coincident to a shift to a starchy diet during human evolution.
For an amylase blood test, a health care professional will take a blood sample from a vein in your arm, using a small needle. 

After the needle is inserted, a small amount of blood will be collected into a test tube or vial. You may feel a little sting when the needle goes in or out. 
This usually takes less than five minutes.
Amylase the hydrolysis of internal alpha-glucosidic linkages in starch and other related oligo- and polysaccharides. 

These enzymes are widespread among the higher plants, animals and micro-organisms.
Cereal alpha-amylases play an important role in the production of beer and other alcoholic beverages.

In humans, alpha-amylase is present in salivary and pancreatic secretions. 
Human pancreatic alpha-amylase (HPA) is a 496 amino acid single polypeptide chain which binds to essential calcium and chloride ions, and is responsible for the hydrolysis of the partially digested starch (smaller oligosaccharides) reaching the gut, into glucose. 
Inhibition of Amylase provides an effective target for the treatment of diabetes.

Uses:
Amylase 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. 

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.
Textile desizing, conversion of starch to glucose sugar in syrups (especially corn syrups), baking (to improve crumb softness and shelf life), dry cleaning (to attack food spots and similar stains).

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.
Amylase is an incredibly versatile enzyme with a wide range of uses across several industries due to its ability to break down complex carbohydrates into simpler sugars. 

In the food and beverage industry, amylase is essential in the production of bread, beer, and other fermented products. 
In bread-making, the enzyme helps break down starches in the flour into simpler sugars, which yeast can then ferment to produce carbon dioxide, causing the dough to rise and resulting in soft, airy bread. 
In brewing, amylase acts on the starches in grains, such as barley, converting them into fermentable sugars that yeast then converts into alcohol and carbon dioxide. 

This enzymatic breakdown is essential in both alcoholic and non-alcoholic beverages, as it enables efficient fermentation, flavor development, and alcohol production.
Another key application of amylase is in the production of high-fructose corn syrup (HFCS), where the enzyme plays a crucial role in converting corn starch into sugars. 
These sugars are further processed to produce HFCS, which is widely used as a sweetener in soft drinks, baked goods, and various processed foods. 

The food industry also relies on amylase for syrup and sugar production, where the enzyme helps increase the sweetness of starch-derived products and improve their functionality in cooking and baking processes.
In the textile industry, Amylase is used as a desizing agent to remove starch-based sizing agents applied to fabrics during the weaving process. 
These starches must be removed before the fabric can undergo further treatments such as dyeing or finishing. 

Amylase helps break down these starches efficiently, allowing for cleaner and smoother fabric that is more suitable for the dyeing process, which results in improved texture and color retention. 
This process is commonly used in cotton and synthetic textiles, contributing to high-quality fabric production.
Amylase also plays an important role in the detergent industry. 

Amylase is included in some laundry detergents and cleaning products to help break down starch-based stains, such as those caused by food or beverages. 
By targeting and breaking down these complex carbohydrate molecules, amylase helps remove stains that would otherwise be difficult to clean, making it an essential enzyme in modern laundry detergents. 
Its use in cleaning products extends beyond clothing, helping to improve the effectiveness of surface cleaners in both household and industrial settings.

In the pharmaceutical industry, amylase is used in enzyme supplements, particularly for individuals with pancreatic insufficiency or other digestive disorders. 
These supplements help patients by aiding the breakdown of starches and other complex carbohydrates, which would otherwise be poorly digested due to a lack of sufficient amylase production. 
By improving digestion, amylase supplements help prevent symptoms such as bloating, indigestion, and malabsorption of nutrients.

Amylase is also critical in the production of biofuels, especially ethanol, where it facilitates the conversion of starch from crops like corn into fermentable sugars. 
These sugars are then fermented by yeast to produce ethanol, a renewable fuel. 
Amylase is integral to the biofuel production process as it ensures that the starch is efficiently converted into a form that can be used by yeast to generate the fuel. 

This process contributes to the growing demand for renewable energy sources and reduces reliance on fossil fuels.
Additionally, amylase is used in the paper and pulp industries to improve the quality of paper products. 
The enzyme is added during the pulp preparation process to break down starches that can interfere with paper production, helping to improve the quality and texture of the final product. 

This application is especially important in the production of high-quality paper products, such as those used in packaging and printing.
In bioremediation, amylase has been explored as a potential tool to help break down organic pollutants in the environment. 
Since amylase can degrade starches and other complex carbohydrates, it could be used in the cleanup of polluted sites, particularly in the remediation of organic waste. 

Its application in environmental sciences is still under research but holds promise for addressing environmental contamination in a sustainable way.
In addition to its widespread industrial uses, amylase plays a vital role in medical and diagnostic applications. 
One such application is in the diagnosis and monitoring of pancreatic disorders. 

Amylase levels are measured in blood and urine tests to help assess conditions like pancreatitis, a condition in which the pancreas becomes inflamed. 
Elevated amylase levels often indicate damage to the pancreas, helping healthcare professionals diagnose and monitor the severity of the disease. 
Similarly, amylase testing can also assist in the diagnosis of conditions such as cystic fibrosis, mumps, and certain gastrointestinal disorders, providing crucial insights into digestive health and enzyme function.

Amylase is also utilized in biotechnology, where it is used in genetic engineering processes to create engineered versions of the enzyme for specific industrial applications. 
For example, genetically modified microorganisms can be designed to produce amylase in large quantities, which is particularly useful for industrial-scale operations. 
These enhanced enzymes are often more efficient and cost-effective, enabling large-scale production of food, biofuels, and other products that require starch conversion. 

This biotechnological innovation has revolutionized the enzyme industry, enabling the production of amylase at a scale and efficiency previously unattainable.
In animal feed, amylase is sometimes added to improve the digestibility of carbohydrates in animal diets. 
Livestock, particularly poultry and swine, often consume diets that contain grains and cereals rich in starches. 

Adding amylase to animal feed helps break down these starches into simpler sugars, improving nutrient absorption and overall feed efficiency. 
This application not only benefits the health and growth of the animals but also reduces waste and enhances the sustainability of livestock farming by optimizing feed use.
Amylase is also used in some wound-care products, particularly for chronic wounds that have a high concentration of necrotic tissue or biofilms. 

In these cases, amylase can help break down starches and other organic material in the wound, aiding in the debridement process. 
This enzymatic action helps remove dead tissue, promoting the healing of the wound and preventing infection. 
The enzyme’s ability to break down complex carbohydrates and other biological substances makes it an effective agent for improving wound care and speeding up recovery times.

Furthermore, in the beverage industry, amylase plays a significant role in the production of non-alcoholic drinks, such as fruit juices and soft drinks. 
It is used to break down starches in certain fruit-based beverages, helping to improve the clarity and sweetness of the final product. 
By breaking down complex carbohydrates into simpler sugars, amylase also helps to reduce the need for additional sweeteners, creating a more natural and healthier product.

Amylase also finds its way into the production of various cosmetics and personal care products. 
The enzyme is sometimes included in facial cleansers and exfoliating treatments, where it helps break down starches and other complex carbohydrates that may accumulate on the skin's surface.
This action can help cleanse the skin, making it smoother and more radiant. 

Additionally, amylase may be used in hair care products to help break down the starches present in products like hair sprays, dry shampoos, and conditioners, contributing to the overall cleanliness and shine of the hair.
Another area where amylase has found use is in the production of specialty chemicals and pharmaceuticals. 
It is often used in the synthesis of certain sugar derivatives and oligosaccharides, which are key components in the production of various chemicals and drugs. 

Amylase can break down starches into these smaller molecules, which can then be used as building blocks for the manufacture of a range of pharmaceutical ingredients, including those used in vaccines, antibiotics, and other therapeutics.
Moreover, amylase is used in various forms of biocatalysis for the production of specialty sugars. This application is particularly useful in the synthesis of sugars that are not easily obtained through traditional chemical processes, such as rare oligosaccharides that may have specific medical or industrial uses. 

By using amylase in biocatalytic reactions, researchers can access sugars and sugar derivatives that might otherwise be difficult or expensive to produce.
In food processing, it is sometimes employed to help prevent spoilage or microbial growth by breaking down starches in certain food products. 
This enzymatic breakdown makes the environment less hospitable to spoilage bacteria, helping to extend the shelf life of products and maintain food quality.

Safety Profile:
One of the most common hazards of amylase is the potential for allergic reactions, particularly in workers who are exposed to large amounts of the enzyme, such as in industrial settings. 
These allergic reactions can range from mild symptoms like skin irritation or respiratory discomfort to more severe reactions such as asthma or anaphylaxis, which may require immediate medical attention. 
Individuals who are allergic to proteins found in amylase, or to components used in its production, may experience symptoms such as itching, rashes, or difficulty breathing. 

In some cases, repeated exposure can lead to sensitization, where an individual’s immune system becomes increasingly reactive to the enzyme.
The powder form of amylase, especially when used in large-scale industrial processes, can present inhalation hazards. 
If inhaled, the enzyme can cause irritation to the respiratory tract, potentially leading to symptoms such as coughing, wheezing, or shortness of breath. 

Prolonged or repeated inhalation of amylase dust can increase the risk of developing respiratory issues, including asthma or other forms of occupational lung disease, particularly in workers in the food, detergent, or biofuel industries. 
To minimize this risk, proper ventilation and protective equipment, such as dust masks or respirators, should be used when handling amylase in its powdered form.

Amylase can cause irritation when it comes into contact with the skin or eyes. While the enzyme itself is not typically corrosive, concentrated forms may lead to redness, itching, or discomfort in sensitive individuals. 
In the case of eye exposure, amylase may cause irritation, leading to symptoms such as watering, redness, or a gritty feeling. 

Prolonged skin contact, especially with concentrated or industrial formulations, may result in dermatitis or other skin conditions. 
To prevent such hazards, protective gloves, goggles, and other personal protective equipment should be worn when handling concentrated forms of amylase.