Talk:Amylase

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Untitled[edit]

There are also BETA and GAMMA amylases..which have EC 3.2.1.2 and 3. ALPHA is .1.. but this is the most "popular" form ie. when someone talks about it they usually mean the α-form. can someone add some information about them?. This article seems too short for a major enzyme.. but I can't think of anything else to add. 218.102.71.16 17:24, 2 February 2006 (UTC)[reply]

There is also no mention of salivary amylase, which is important in the digestive tract of many vertebrates. I don't know enough about it but somebody should add at least a mention.

This whole article is highly focused on the human/animal biology of amylase. However, there are many other sources of amylase, and this needs restructured. Henry Troup 00:23, 2 Feb 2005 (UTC)

β-amylase: A Simple Method to Differentiate between α- and β-Amylase <-- describes a key difference in their enzymatic activity. recent article that discusses the idea that β-amylase in barley "plays an important role in determining good malting quality".

γ-amylase (entry at the Integrated relational Enzyme database) is also known as acid alpha-glucosidase and lysosomal alpha-glucosidaseOMIM. In humans, the lysosomal enzyme is associated with glycogen storage disease type II (Pompe disease).

There is a lot of overlap in nomenclature, but γ-amylase (EC 3.2.1.3 ) is not acid α-glucosidase (EC 3.2.1.20 ) Novangelis 17:37, 25 September 2006 (UTC)[reply]

There is also no mention of salivary amylase, which is important in the digestive tract of many vertebrates. I don't know enough about it but somebody should add at least a mention.

Reorganization[edit]

  • I've created a "classification" section to deal with the functions of the various amylases. Are there any other enzymes that belong on this page?
  • There is no entry for glycogenase. Should it redirect here?
  • I separted sections for human physiology and human pathology. With further revision, a better pattern may emerge.
  • I used the Edit box "α,β,γ", replacing HTML, based on style guides. Most of the HTML versions were my entries. I'm not trying to srart a war.
  • I (or someone else) should create a maltotriose entry, unless someone thinks it would be better to create one trisaccharide page. Thoughts?

Novangelis 14:45, 23 September 2006 (UTC)[reply]

Discovery[edit]

Someone inserted that amylase was invented in 1841[1]. I could not verify this. Does anyone have historical references on the subject? JFW | T@lk 13:59, 17 January 2006 (UTC)[reply]

I'm not sure about the time of the first documented use of a mixture that has amylase activity, but "amylase" was definately not invented then. Good call. -- Boris 15:49, 17 January 2006 (UTC)[reply]

Actually it was JWSchmidt who reverted, but it would still be interesting to write something about the history of this enzyme :-) > JFW | T@lk 16:39, 17 January 2006 (UTC)[reply]


"1831 Erhard Friedrich Leuchs (1800-1837) describes the diastatic action of salivary ptyalin (amylase) on starch."[2]

"The modern history of enzymes dates back to 1833 when, in the journal Annales de Chemie et de Physique, the French chemists Anselme Payen and Jean-Franois Persoz described the isolation of an amylase complex from germinating barley and named it diastase." [3]

"1862 DANIELEWSKI separated pancreatic amylase from trypsin" [4] --JWSchmidt 17:10, 17 January 2006 (UTC)[reply]

I put the above back into the article, revised. It still needs complete refs and probably other work. --Una Smith (talk) 01:43, 25 October 2008 (UTC)[reply]

Alternative name[edit]

I have heard somewhere that pancreatic amylase is also known as amylopsin. Is that right?


Conflicting Optimal pH[edit]

Ptylins optimal pH is listed as 5.6 - 6.9. However, BRENDA (enzyme database) lists Alpha-Amylase optimal pH range, in humans, between 6.9 and 7.1 (Reference 393476). Can anyone double check this against another source?

industry[edit]

Can you please add uses of amylase in industry . .fermenters etc?? —The preceding unsigned comment was added by 194.204.127.119 (talk) 17:09, 7 December 2006 (UTC).[reply]

Not sure...[edit]

...whether to add this or not: should this article note that dietary supplement Phaseolamin works by inhibiting alpha-amylase? JulesH 19:12, 18 March 2007 (UTC)[reply]

Protected[edit]

For some odd reason, this article suffers from frequent low-grade vandalism. I'm going to try {{sprotected2}} for a little bit. JFW | T@lk 15:54, 30 April 2007 (UTC)[reply]

Endorsed. It's on my watchlist, but there's only so much one can do :( Fvasconcellos (t·c) 16:10, 30 April 2007 (UTC)[reply]

Structures[edit]

  • Just one thing...both the pancriatic and salivary amyase diagrams look the same...am I wrong? Great page though =D 90.241.161.135 16:03, 18 September 2007 (UTC)[reply]
    • The structures of both isoforms of the enzyme are extremely similar—they're supposed to look almost the same :) Fvasconcellos (t·c) 02:31, 19 September 2007 (UTC)[reply]

Totally wrong[edit]

The article gets it totally wrong about what is β- and γ-Amylase. Just click on the link and see for yourself that EC 3.2.1.2 is limited to bacteria and plants, and EC 3.2.1.3 is limited to fungi. Likewise the proteins mentioned there in the article don't have amylase names when you look them up in UniProt. --Ayacop (talk) 15:04, 18 December 2008 (UTC) I also want to add that in the beta-amylase profile, there is mention of the enzyme working from the non-reducing end. This sentence is contradictory, for the reason that it is being seperated in the middle. —Preceding unsigned comment added by 74.15.175.192 (talk) 15:57, 6 February 2009 (UTC)[reply]

pH optimum[edit]

At gamma-amylase you have _Unlike the other forms of amylase, γ-amylase is most efficient in acidic environments and has an optimum pH of 3._ and at beta-amylase you have that the pH optimum is 4-5, which is pretty much acidic. I'll re-writte that sentence. TH 08:53, 23 November 2012 (UTC) — Preceding unsigned comment added by 158.194.65.113 (talk)

Refer as 'Glucose' not 'Sugars'[edit]

It is best to refer as sugar (in chemistry) as Glucose 78.146.124.198 (talk) 20:12, 8 October 2014 (UTC)[reply]

Thanks for the suggestion. If you're referring to the first sentence ("Amylase is an enzyme that catalyses the hydrolysis of starch into sugars"), the problem is that many amylases hydrolyse starch into maltose, short oligosaccharides, and/or other sugars instead of or in addition to glucose. Even glucoamylases produce sugars other than glucose from starch's branchpoints. Adrian J. Hunter(talk•contribs) 01:10, 9 October 2014 (UTC)[reply]

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