Amylase

Uses

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. 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.

α-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). It 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 alpha-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, it is known that the salivary alpha-amylase response to stress is reduced in intensity in people with occupational burnout.

Other uses

An inhibitor of alpha-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.

Hyperamylasemia

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.

History

In 1831, Erhard Friedrich Leuchs (1800–1837) described the hydrolysis of starch by saliva, due to the presence of an enzyme in saliva, "ptyalin", an amylase. It was named after the Ancient Greek name for saliva: πτύαλον - ptyalon.

The modern history of enzymes began in 1833, when French chemists Anselme Payen and Jean-François Persoz isolated an amylase complex from germinating barley and named it "diastase". It is from this term that all subsequent enzyme names tend to end in the suffix -ase.

In 1862, Russian biochemist Aleksandr Yakovlevich Danilevsky (1838–1923) separated pancreatic amylase from trypsin.

Evolution

Salivary amylase

Saccharides 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.

Like in other mammals, the pancreatic alpha-amylase AMY2 was duplicated multiple times. One event allowed it to evolve salivary specificity, leading to the production of amylase in the saliva (named in humans as AMY1). The 1p21.1 region of human chromosome 1 contains many copies of these genes, variously named AMY1A, AMY1B, AMY1C, AMY2A, AMY2B, and so on.

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 AMY1 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 AMY1 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.