Amylase
An amylase (/ˈæmɪleɪs/) 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.
| Alpha-amylase | |
|---|---|
| Identifiers | |
| EC no. | 3.2.1.1 |
| CAS no. | 9000-90-2 |
| Databases | |
| IntEnz | IntEnz view |
| BRENDA | BRENDA entry |
| ExPASy | NiceZyme view |
| KEGG | KEGG entry |
| MetaCyc | metabolic pathway |
| PRIAM | profile |
| PDB structures | RCSB PDB PDBe PDBsum |
| Gene Ontology | AmiGO / QuickGO |
| Beta-amylase | |
|---|---|
| Identifiers | |
| EC no. | 3.2.1.2 |
| CAS no. | 9000-91-3 |
| Databases | |
| IntEnz | IntEnz view |
| BRENDA | BRENDA entry |
| ExPASy | NiceZyme view |
| KEGG | KEGG entry |
| MetaCyc | metabolic pathway |
| PRIAM | profile |
| PDB structures | RCSB PDB PDBe PDBsum |
| Gene Ontology | AmiGO / QuickGO |
Classification edit
| α-amylase | β-amylase | γ-amylase | |
|---|---|---|---|
| Source | Animals, plants, microbes | Plants, microbes | Animals, microbes |
| Tissue | Salivary gland, pancreas | Seeds, fruits | Small intestine |
| Cleavage site | Random α-1,4 glycosidic bond | Second α-1,4 glycosidic bond | Last α-1,4 glycosidic bond |
| Reaction products | Maltose, dextrin, etc. | Maltose | Glucose |
| Optimum pH | 6.7–7.0 | 5.4–5.5 | 4.0–4.5 |
| Optimum temperature in brewing | 68–74 °C (154–165 °F) | 58–65 °C (136–149 °F) | 63–68 °C (145–155 °F) |
α-Amylase edit
The α-amylases (EC 3.2.1.1 ) (CAS 9014-71-5) (alternative names: 1,4-α-D-glucan glucanohydrolase; glycogenase) 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. They belong to glycoside hydrolase family 13 (https://www.cazypedia.org/index.php/Glycoside_Hydrolase_Family_13).
Because it can act anywhere on the substrate, α-amylase tends to be faster-acting than β-amylase. In animals, it is a major digestive enzyme, and its optimum pH is 6.7–7.0.[3]
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).
β-Amylase edit
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. The optimum pH for β-amylase is 4.0–5.0.[4]
γ-Amylase edit
γ-Amylase (EC 3.2.1.3 ) (alternative names: Glucan 1,4-a-glucosidase; amyloglucosidase; exo-1,4-α-glucosidase; glucoamylase; lysosomal α-glucosidase; 1,4-α-D-glucan glucohydrolase) will cleave α(1–6) glycosidic linkages, as well as the last α-1,4 glycosidic bond at the nonreducing end of amylose and amylopectin, yielding glucose. The γ-amylase has the most acidic optimum pH of all amylases because it is most active around pH 3. They belong to a variety of different GH families, such as glycoside hydrolase family 15 in fungi, glycoside hydrolase family 31 of human MGAM, and glycoside hydrolase family 97 of bacterial forms.
Uses edit
Fermentation edit
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.[5] 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 edit
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.[6][failed verification]
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[7] or asthma.[8]
Molecular biology edit
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 edit
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.[9]
Other uses edit
An inhibitor of alpha-amylase, called phaseolamin, has been tested as a potential diet aid.[10]
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.[11]
Hyperamylasemia edit
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),[12] 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.[13]
History edit
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.[14][15] 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".[16][17] It is from this term that all subsequent enzyme names tend to end in the suffix -ase.
In 1862, Alexander Jakulowitsch Danilewsky (1838–1923) separated pancreatic amylase from trypsin.[18][19]
Evolution edit
Salivary amylase edit
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.[20]
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.[21]
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.[22]
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.[22]
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.[22]
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.[22]
Variations of amylase copy number in dogs mirrors that of human populations, suggesting they acquired the extra copies as they followed humans around.[23] 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.[20]
References edit
- ^ Ramasubbu N, Paloth V, Luo Y, Brayer GD, Levine MJ (May 1996). "Structure of human salivary alpha-amylase at 1.6 Å resolution: implications for its role in the oral cavity". Acta Crystallographica D. 52 (3): 435–446. doi:10.1107/S0907444995014119. PMID 15299664.
- ^ Rejzek M, Stevenson CE, Southard AM, Stanley D, Denyer K, Smith AM, Naldrett MJ, Lawson DM, Field RA (March 2011). "Chemical genetics and cereal starch metabolism: structural basis of the non-covalent and covalent inhibition of barley β-amylase". Molecular BioSystems. 7 (3): 718–730. doi:10.1039/c0mb00204f. PMID 21085740. S2CID 45819617.
- ^ "Effects of pH (Introduction to Enzymes)". worthington-biochem.com. Retrieved 17 May 2015.
- ^ "Amylase, Alpha, I.U.B.: 3.2.1.11,4-α-D-Glucan glucanohydrolase".
- ^ Wadler J (8 September 2009). "Chew It Up, Spit It Out, Then Brew. Cheers!". New York Times. Retrieved 27 March 2013.
- ^ Maton A, Hopkins J, McLaughlin CW, Johnson S, Warner MQ, LaHart D, Wright JD (1993). Human Biology and Health. Englewood Cliffs, NJ: Prentice Hall. ISBN 0-13-981176-1.
- ^ Morren MA, Janssens V, Dooms-Gossens A, Van Hoeyveld E, Cornelis A, De Wolf-Peeters C, Heremans A (November 1993). "alpha-Amylase, a flour additive: an important cause of protein contact dermatitis in bakers". Journal of the American Academy of Dermatology. 29 (5 Pt 1): 723–728. doi:10.1016/0190-9622(93)70237-n. PMID 8227545.
- ^ Park HS, Kim HY, Suh YJ, Lee SJ, Lee SK, Kim SS, Nahm DH (September 2002). "Alpha amylase is a major allergenic component in occupational asthma patients caused by porcine pancreatic extract". The Journal of Asthma. 39 (6): 511–516. doi:10.1081/jas-120004918. PMID 12375710. S2CID 23522631.
- ^ . Anthera Pharmaceuticals. Archived from the original on 18 July 2015. Retrieved 21 July 2015.
- ^ Udani J, Hardy M, Madsen DC (March 2004). (PDF). Alternative Medicine Review. 9 (1): 63–69. PMID 15005645. Archived from the original (PDF) on 2011-07-28.
- ^ Mapp CE (May 2001). "Agents, old and new, causing occupational asthma". Occupational and Environmental Medicine. 58 (5): 354–360, 290. doi:10.1136/oem.58.5.354. PMC 1740131. PMID 11303086.
- ^ "Acute Pancreatitis – Gastrointestinal Disorders". Merck Manuals Professional Edition. Merck.[permanent dead link]
- ^ "First Biomarker for Human Sleepiness Identified". Record. Washington University in St. Louis. 25 January 2007.
- ^
- Leuchs EF (1831). "Wirkung des Speichels auf Stärke" [Effect of saliva on starch]. Poggendorff's Annalen der Physik und Chemie. 22 (8): 623. Bibcode:1831AnP....98..623L. doi:10.1002/andp.18310980814. (Modern citation: Annalen der Physik 98 (8): 623.)
- Leuchs EF (1831). "Über die Verzuckerung des Stärkmehls durch Speichel" [On the saccharification of powdered starch by saliva]. Archiv für die gesammte Naturlehre. 21: 105–107.
- ^ . pasteur.fr. 8 April 2002. Archived from the original on 24 September 2015. Retrieved 17 May 2015.
- ^ Payen A, Persoz JF (1833). "Mémoire sur la diastase, les principaux produits de ses réactions et leurs applications aux arts industriels" [Memoir on diastase, the principal products of its reactions and their applications to the industrial arts]. Annales de chimie et de physique. 2nd series. 53: 73–92.
- ^ . Archived from the original on 5 December 2008.
- ^ Danilewsky AJ (1862). "Über specifisch wirkende Körper des natürlichen und künstlichen pancreatischen Saftes" [On the specifically-acting principles of natural and artificial pancreatic fluid]. Virchows Archiv für Pathologische Anatomie und Physiologie und für Klinische Medizin. 25: 279–307. Abstract (in English).
- ^ . navi.net. Archived from the original on 2022-01-10. Retrieved 2008-10-25.
- ^ a b Pajic P, Pavlidis P, Dean K, Neznanova L, Romano RA, Garneau D, et al. (May 2019). "Independent amylase gene copy number bursts correlate with dietary preferences in mammals". eLife. 8. doi:10.7554/eLife.44628. PMC 6516957. PMID 31084707.
- ^ Vuorisalo T, Arjamaa O (March–April 2010). . American Scientist. 98 (2): 140. doi:10.1511/2010.83.140. Archived from the original on 2016-03-04. Retrieved 2015-08-15.
- ^ a b c d Perry GH, Dominy NJ, Claw KG, Lee AS, Fiegler H, Redon R, Werner J, Villanea FA, Mountain JL, Misra R, Carter NP, Lee C, Stone AC (October 2007). "Diet and the evolution of human amylase gene copy number variation". Nature Genetics. 39 (10): 1256–1260. doi:10.1038/ng2123. PMC 2377015. PMID 17828263.
- ^ Arendt M, Cairns KM, Ballard JW, Savolainen P, Axelsson E (November 2016). "Diet adaptation in dog reflects spread of prehistoric agriculture". Heredity. 117 (5): 301–306. doi:10.1038/hdy.2016.48. PMC 5061917. PMID 27406651.