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A diastase (/ˈdaɪəsteɪz/; from Greek διαστασις, "separation") is any one of a group of enzymes which catalyses the breakdown of starch into maltose. Alpha 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 means any α-, β-, or γ-amylase (all of them 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.

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

References

^ Gray, G.M. (1975). "Carbohydrate digestion and absorption". New England Journal of Medicine 292 (23): 1225–1230. doi:10.1056/NEJM197506052922308. PMID 1093023.
^ See:
- Hill, Robert; Needham, Joseph (1970). The Chemistry of Life: Eight Lectures on the History of Biochemistry. London: Cambridge University Press. p. 17.
- Silverman, Richard B. (2002). The Organic Chemistry of Enzyme-catalyzed Reactions (2nd ed.). London: Academic Press. p. 1.
- Stenesh, Jochanan (1998). Biochemistry 2. New York: Plenum. p. 83.
- Meyers, Robert A., ed. (1995). Molecular Biology and Biotechnology: A Comprehensive Desk Reference. New York: Wiley-VCH. p. 296.
^ 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"
^ Oliver, Garrett (2011). The Oxford companion to beer. Oxford: Oxford University Press. p. 49. ISBN 0199912106. 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.

Payen, A. et J.-F. Persoz (1833)

"Mémoire sur la diastase, les principaux produits de ses réactions et leurs applications aux arts industriels", Annales de chimie et de physique, 2nd series, 53 : 73–92.

External links

Diastase at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

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English Journal

Milk glucosidase activity enables suckled pup starch digestion.

Nichols BL1, Diaz-Sotomayor M2, Avery SE3, Chacko SK4, Hadsell DL5, Baker SS6, Hamaker BR7, Yan LK8, Lin HM9,10, Quezada-Calvillo R11,12.
Molecular and cellular pediatrics.Mol Cell Pediatr.2016 Dec;3(1):4. doi: 10.1186/s40348-016-0032-z. Epub 2016 Feb 1.
ᅟ: Starch requires six enzymes for digestion to free glucose: two amylases (salivary and pancreatic) and four mucosal maltase activities; sucrase-isomaltase and maltase-glucoamylase. All are deficient in suckling rodents.OBJECTIVE: The objective of this study is to test (13)C-starch digestion befo
PMID 26830109

Honey: Chemical composition, stability and authenticity.

da Silva PM1, Gauche C2, Gonzaga LV2, Costa AC2, Fett R2.
Food chemistry.Food Chem.2016 Apr 1;196:309-23. doi: 10.1016/j.foodchem.2015.09.051. Epub 2015 Sep 16.
The aim of this review is to describe the chemical characteristics of compounds present in honey, their stability when heated or stored for long periods of time and the parameters of identity and quality. Therefore, the chemical characteristics of these compounds were examined, such as sugars, prote
PMID 26593496

β-amylase 1 (BAM1) degrades transitory starch to sustain proline biosynthesis during drought stress.

Zanella M1, Borghi GL2, Pirone C2, Thalmann M3, Pazmino D3, Costa A4, Santelia D3, Trost P2, Sparla F5.
Journal of experimental botany.J Exp Bot.2016 Apr;67(6):1819-26. doi: 10.1093/jxb/erv572. Epub 2016 Jan 20.
During photosynthesis of higher plants, absorbed light energy is converted into chemical energy that, in part, is accumulated in the form of transitory starch within chloroplasts. In the following night, transitory starch is mobilized to sustain the heterotrophic metabolism of the plant. β-amylases
PMID 26792489

Japanese Journal

Vaginal clear cell carcinoma in a Japanese Black cow

Journal of Veterinary Medical Science 78(5), 901-903, 2016
NAID 130005154287

分泌性髄膜腫の 1 例:—圧挫標本の細胞像について—

日本臨床細胞学会雑誌 55(1), 58-59, 2016
NAID 130005126753

Vaginal clear cell carcinoma in a Japanese Black cow

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★リンクテーブル★

リンク元	「アミラーゼ」「ジアスターゼ」

「アミラーゼ」

　　[★]

英: amylase, AMY, Amy
同: ジアスターゼ diastase
関: 唾液アミラーゼ

図：LAB.599(血清アミラーゼ異常をきたす疾患)

基準値

4–400 U/L (HIM.Appendix)

判別

検査の本

基準上限以上(高値)(高アミラーゼ血症)

[高頻度]急性膵炎、慢性膵炎
[可能性]膵嚢胞、膵癌、総胆管結石、Vater乳頭癌、急性耳下腺炎、唾石、消化管穿孔、腸閉塞、腹膜炎、子宮外妊娠、アミラーゼ産生腫瘍(肺癌、卵巣癌、卵管癌など)、マクロアミラーゼ血症、慢性腎不全、ショック、ERCP後

基準下限以下(減少)(低アミラーゼ血症)

[可能性]膵全摘後、慢性膵炎や膵癌による膵実質の荒廃、唾液腺摘出後

異常値を示すメカニズム

OLM.265

高アミラーゼ血症

原因：

膵臓

膵実質の破壊病変：膵炎(原発性・続発性(穿通性十二指腸潰瘍、腹膜炎))、慢性膵炎(頻度低い)、膵癌(頻度低い)
膵液分泌経路の閉塞：膵管・総胆管・Vater乳頭部の閉塞によりAMYが血流に逆流する。
腸管からの吸収増加：小腸上位に腸閉塞が起こると、十二指腸の拡張によりVater乳頭部を圧迫し、閉塞性増加を来し、また十二指腸の壊死がおこると分泌されたアミラーゼが再吸収されてしまう。
腹腔からの吸収：消化管穿孔においてはアミラーゼを含む消化液が腹腔に漏出し、これが腹膜より吸収されるため。(QB.A-353)

唾液腺

唾液腺の病変：ムンプス、耳下腺腫瘍、唾石

その他

肝障害：肝炎、アルコール肝障害。この場合S型AMYが上昇
肺癌による異所性AMY：肺癌や卵巣癌でS型AMYが産生される。
子宮外妊娠破裂：S型AMy上昇
腎不全：血清AMYの約1/3は腎糸球体を通して尿中に排泄されるが、腎機能低下例では増加する
マクロアミラーゼ血症：血清中のAMYの一部が免疫グロブリンや多糖体吐血尾久して大きな分子集団を作ることがある。
心因性拒食症、胸痛、手術後：S型AMY上昇

低アミラーゼ血症

膵や唾液腺の摘出後、慢性膵炎や膵癌による膵実質の荒廃

血清アミラーゼとアイソザイムの異常

LAB.599

膵型アミラーゼ活性の異常	活性増加	急性膵炎
		慢性膵炎増悪
		膵癌、膵嚢腫、膵仮性嚢胞などでの随伴性膵炎
		胆道系の炎症性疾患
		ERCP後、PS試験後
		ステロイドホルモン投与後
		唾液腺型アミラーゼ活性低下による相対的な膵型優位
	活性低下	慢性膵炎
		膵癌(末期)
		膵切除後
唾液腺型アミラーゼ活性の異常	活性増加	流行性耳下腺炎
		術後、外傷後、ショック後、熱傷後
		糖尿病ケトアシドーシス
		人工心肺使用後
		アミラーゼ産生腫瘍(肺癌、卵巣癌など)
		肺炎、肺結核
		腎疾患
		唾液腺造影後
		膵型アミラーゼ活性低下による相対的な唾液腺型優位
	活性低下	放射線治療後(下顎部、頚部など)
	活性低下	シェーグレン症候群
膵型・唾液腺型共に活性増加		腎不全
膵型・唾液腺型共に活性増加		肝硬変、慢性肝炎の一部
膵型・唾液腺型に分類不能の活性増加		マクロアミラーゼ血症
膵型・唾液腺型に分類不能の活性増加		アミラーゼ産生腫瘍の一部

「ジアスターゼ」

　　[★]

英: diastase
商: ジアスターゼ; FK配合散、HM散、KM散、TM配合散、ジアス、NIM配合散、OM配合散、YM散、タフマックE配合、ビットサン、ピーマーゲン配合散、リーダイMM配合散、重散
関: アミラーゼ

麦芽由来アミラーゼ

[1] Gray, G.M. (1975). "Carbohydrate digestion and absorption". New England Journal of Medicine 292 (23): 1225–1230. doi:10.1056/NEJM197506052922308. PMID 1093023.

[2] See:

Hill, Robert; Needham, Joseph (1970). The Chemistry of Life: Eight Lectures on the History of Biochemistry. London: Cambridge University Press. p. 17.

Silverman, Richard B. (2002). The Organic Chemistry of Enzyme-catalyzed Reactions (2nd ed.). London: Academic Press. p. 1.

Stenesh, Jochanan (1998). Biochemistry 2. New York: Plenum. p. 83.

Meyers, Robert A., ed. (1995). Molecular Biology and Biotechnology: A Comprehensive Desk Reference. New York: Wiley-VCH. p. 296.

[3] Hill, Robert; Needham, Joseph (1970). The Chemistry of Life: Eight Lectures on the History of Biochemistry. London: Cambridge University Press. p. 17.

[4] Silverman, Richard B. (2002). The Organic Chemistry of Enzyme-catalyzed Reactions (2nd ed.). London: Academic Press. p. 1.

[5] Stenesh, Jochanan (1998). Biochemistry 2. New York: Plenum. p. 83.

[6] Meyers, Robert A., ed. (1995). Molecular Biology and Biotechnology: A Comprehensive Desk Reference. New York: Wiley-VCH. p. 296.

[3] 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).

[4] Payen & Persoz (1833), pages 75-76.

[5] Etymology of "diastase"

[6] Oliver, Garrett (2011). The Oxford companion to beer. Oxford: Oxford University Press. p. 49. ISBN 0199912106. 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.

[7] 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.

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案内

案内

diastase