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1 Clinical significance  





2 See also  





3 References  





4 External links  














Diastase






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From Wikipedia, the free encyclopedia
 


Adiastase (/ˈdəstz/; from Greek διάστασις, "separation") is any one of a group of enzymes that catalyses the breakdown of starch into maltose. For example, the diastase α-Amylase degrades starch to a mixture of the disaccharide maltose; the trisaccharide maltotriose, which contains three α (1-4)-linked glucose residues; and oligosaccharides, known as dextrins, that contain the α (1-6)-linked glucose branches.[1]

Diastase was the first enzyme discovered.[2] It was extracted from malt solution in 1833 by Anselme Payen and Jean-François Persoz, chemists at a French sugar factory.[3] The name "diastase" comes from the Greek word διάστασις (diastasis) (a parting, a separation), because when beer mash is heated, the enzyme causes the starch in the barley seed to transform quickly into soluble sugars and hence the husk to separate from the rest of the seed.[4][5] Today, "diastase" refers to any α-, β-, or γ-amylase (all of which are hydrolases) that can break down carbohydrates.[6]

The commonly used -ase suffix for naming enzymes was derived from the name diastase.[7]

When used as a pharmaceutical drug, diastase has the ATC code A09AA01 (WHO).

Amylases can also be extracted from other sources including plants, saliva and milk.

Clinical significance

[edit]

Urine diastase is useful in diagnosing uncertain abdominal cases (especially when pancreatitis is suspected), stones in the common bile duct (choledocholithiasis), jaundice and in ruling out post-operative injury to the pancreas; provided that the diastase level is correlated with clinical features of the patient.[8]

Diastase is also used in conjunction with periodic acid–Schiff stain in histology. For example, glycogen is darkly stained by PAS but can be dissolved by diastase. Fungi, on the other hand, stain darkly with PAS even after treatment by diastase.

See also

[edit]

References

[edit]
  1. ^ Gray, G.M. (1975). "Carbohydrate digestion and absorption". New England Journal of Medicine. 292 (23): 1225–1230. doi:10.1056/NEJM197506052922308. PMID 1093023.
  • ^ See:
  • Silverman, Richard B. (2002). The Organic Chemistry of Enzyme-catalyzed Reactions (2nd ed.). London: Academic Press. p. 1. ISBN 9780126437317.
  • Stenesh, Jochanan (1998). Biochemistry. Vol. 2. New York: Plenum. p. 83. ISBN 9780306457333.
  • Meyers, Robert A., ed. (1995). Molecular Biology and Biotechnology: A Comprehensive Desk Reference. New York: Wiley-VCH. p. 296. ISBN 9780471186342.
  • ^ Payen & Persoz (1833), page 77. Payen and Persoz found diastase in the seeds of barley, oats, and wheat, as well as in potatoes (Payen & Persoz (1833), page 76).
  • ^ Payen & Persoz (1833), pages 75-76.
  • ^ Etymology of "diastase"[usurped]
  • ^ Oliver, Garrett (2011). The Oxford Companion to Beer. Oxford: Oxford University Press. p. 49. ISBN 978-0199912100. Retrieved 2013-12-27. Most of the activity of diastase can be attributed to the activities of two enzymes, alpha and beta amylase, and, to a lesser extent, gamma amylase (together, the amylases), although many other enzymes are also present.
  • ^ The naming of enzymes using the suffix "-ase" has been traced to French scientist Émile Duclaux (1840-1904), who intended to honor the discoverers of diastase by introducing the practice in his book Traité de Microbiologie, vol. 2 (Paris, France: Masson and Co., 1899), Chapter 1, especially page 9.
  • ^ Foged, Jens (March 1935). "The diagnostic value of urine diastase". The American Journal of Surgery. 27 (3): 439–446. doi:10.1016/S0002-9610(35)91022-4.
  • [edit]
    Retrieved from "https://en.wikipedia.org/w/index.php?title=Diastase&oldid=1210867137"

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    This page was last edited on 28 February 2024, at 18:55 (UTC).

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