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Title: Amylase  
Author: World Heritage Encyclopedia
Language: English
Subject: Sphincter of Oddi dysfunction, Enzyme, Diastase, Human digestive system, List of biomolecules
Collection: Chemical Pathology, Ec 3.2.1, Enzymes, Food Additives, Saliva
Publisher: World Heritage Encyclopedia


Amylase is an enzyme that catalyses the hydrolysis of starch 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. As diastase, amylase was the first enzyme to be discovered and isolated (by Anselme Payen in 1833).[1] Specific amylase proteins are designated by different Greek letters. All amylases are glycoside hydrolases and act on α-1,4-glycosidic bonds.


  • Classification 1
    • α-Amylase 1.1
    • β-Amylase 1.2
    • γ-Amylase 1.3
  • Uses 2
    • Fermentation 2.1
    • Flour additive 2.2
    • Molecular biology 2.3
    • Other uses 2.4
  • Hyperamylasemia 3
  • History 4
  • Human evolution 5
  • References 6
  • External links 7



Human salivary amylase: calcium ion visible in pale khaki, chloride ion in green. PDB [2]
EC number
CAS number 9000-90-2
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

The α-amylases (EC ) (CAS# 9014-71-5) (alternative names: 1,4-α-D-glucan glucanohydrolase; glycogenase) are calcium metalloenzymes, completely unable to function in the absence of calcium. By acting at random locations along the starch chain, α-amylase breaks down long-chain carbohydrates, ultimately yielding 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, 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-amylases form is also found in plants, fungi (ascomycetes and basidiomycetes) and bacteria (Bacillus)


Structure of barley beta-amylase. PDB [4]
EC number
CAS number 9000-91-3
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

Another form of amylase, β-amylase (EC ) (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.

Both α-amylase and β-amylase are present in seeds; β-amylase is present in an inactive form prior to digestive tract. The optimum pH for β-amylase is 4.0–5.0[5]


Gamma-Amylase. Glucan 1,4-alpha-glucosidase
EC number
CAS number 9032-08-0
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

γ-Amylase (EC ) (alternative names: Glucan 1,4-α-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 linkages at the nonreducing end of amylose and amylopectin, yielding glucose. The γ-amylase has most acidic optimum pH of all amylases because it is most active around pH 3.



Alpha and beta amylases are important in brewing beer and liquor made from sugars derived from starch. In fermentation, yeast ingest sugars and excrete alcohol. 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 is no longer in general use.

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 alcohol and CO2. 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 sour dough. 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]

Alpha 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

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.

Other uses

An inhibitor of alpha-amylase, called phaseolamin, has been tested as a potential diet aid.[9]

When used as a food additive, amylase has E number E1100, and may be derived from swine pancreas or mould mushroom.

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.[10]


Blood serum amylase may be measured for purposes of medical diagnosis. A higher than normal concentration may reflect one of several medical conditions, including acute inflammation of the pancreas (it may be measured concurrently with the more specific lipase),[11] but also 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.[12]


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.[13][14] 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".[15][16] In 1862, Alexander Jakulowitsch Danilewsky (1838–1923) separated pancreatic amylase from trypsin.[17][18]

Human evolution

Carbohydrates are a food source rich in energy. Following the Agricultural Revolution 12,000 years ago, human diet began to rely more on plant and animal domestication in place of hunting and gathering. This shift also symbolizes the beginning of a diet composed of 49% carbohydrates as opposed to the previous 35% observed in Paleolithic humans. As such, starch became a staple of human diet. Large polymers such as starch are partially hydrolyzed in the mouth by the enzyme amylase before being cleaved further into sugars. Therefore, humans that contained amylase in the saliva would benefit from increased ability to digest starch more efficiently and in higher quantities. 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

  • Molecule of the month February 2006 at the Protein Data Bank.
  • Nutrition Sciences 101 at University of Arizona.
  • Amylase at Lab Tests Online.
  • Amylase: analyte monograph – The Association for Clinical Biochemistry and Laboratory Medicine.

External links

  1. ^ (1) Robert Hill and Joseph Needham, The Chemistry of Life: Eight Lectures on the History of Biochemistry (London, England: Cambridge University Press, 1970), page 17 ; (2) Richard B. Silverman, The Organic Chemistry of Enzyme-catalyzed Reactions, 2nd ed. (London, England: Academic Press, 2002), page 1 ; (3) Jochanan Stenesh, Biochemistry, vol. 2 (New York, New York: Plenum, 1998), page 83 ; (4) Robert A. Meyers, ed., Molecular Biology and Biotechnology: A Comprehensive Desk Reference (New York, New York: Wiley-VCH, 1995), page 296.
  2. ^ Ramasubbu, N.; Paloth, V.; Luo, Y.; Brayer, G. D.; Levine, M. J. (1996). "Structure of Human Salivary α-Amylase at 1.6 Å Resolution: Implications for its Role in the Oral Cavity". Acta Crystallographica Section D Biological Crystallography 52 (3): 435–446.  
  3. ^ Effects of pH (Introduction to Enzymes)
  4. ^ Rejzek, M.; Stevenson, C. E.; Southard, A. M.; Stanley, D.; Denyer, K.; Smith, A. M.; Naldrett, M. J.; Lawson, D. M.; Field, R. A. (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.  
  5. ^ "Amylase, Alpha" , I.U.B.:,4-α-D-Glucan glucanohydrolase.
  6. ^ Maton, Anthea; Jean Hopkins; Charles William McLaughlin; Susan Johnson; Maryanna Quon Warner; David LaHart; Jill D. Wright (1993). Human Biology and Health. Englewood Cliffs, New Jersey, USA: Prentice Hall.  
  7. ^ "alpha-Amylase, a flour additive: an important cause of protein contact dermatitis in bakers". 
  8. ^ "Alpha amylase is a major allergenic component in occupational asthma patients caused by porcine pancreatic extract". 
  9. ^ Udani J, Hardy M, Madsen DC (March 2004). "Blocking carbohydrate absorption and weight loss: a clinical trial using Phase 2 brand proprietary fractionated white bean extract". Altern Med Rev 9 (1): 63–9.  
  10. ^ Mapp CE (May 2001). "Agents, old and new, causing occupational asthma". Occup Environ Med 58 (5): 354–60, 290.  
  11. ^
  12. ^ "First Biomarker for Human Sleepiness Identified", Record of Washington University in St. Louis, January 25, 2007
  13. ^ Erhard Friedrich Leuchs (1831) "Wirkung des Speichels auf Stärke" (Effect of saliva on starch), Poggendorff's Annalen der Physik und Chemie, vol. 22, page 623 (modern citation: Annalen der Physik, vol. 98, no. 8, page 623). See also: Erhard Friedrich Leuchs (1831) "Über die Verzuckerung des Stärkmehls durch Speichel" (On the saccharification of powdered starch by saliva), Archiv für die Gesammte Naturlehre (Archive for All Science), vol. 21, pages 105–107.
  14. ^ History of biology 1800–1849
  15. ^ Anselme Payen and Jean-François Persoz (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. 
  16. ^ Industrial Enzymes for Food Production
  17. ^ Danilewsky (1862) "Über specifisch wirkende Körper des natürlichen und künstlichen pancreatischen Saftes" (On the specifically-acting principles of the natural and artificial pancreatic juice), Virchows Archiv für pathologische Anatomie und Physiologie, und für klinische Medizin, vol. 25, pages 279–307. Abstract (in English).
  18. ^ A History of Fermentation and Enzymes
  19. ^ Vuorisalo, Timo; Arjamaa, Olli (March–April 2010). "Gene-Culture Coevolution and Human Diet". American Scientist 98 (2): 140.  
  20. ^ a b 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): 1256–60.  


However, not all humans possess the same number of copies of the AMY1 gene. Populations known to rely more on carbohydrates exhibit 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 2-3 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 population 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.[20]


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