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any of a group of proteins found in saliva and pancreatic juice and parts of plants; help convert starch to sugar

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アミラーゼ(でんぷん糖化酵素)

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/11/04 23:57:26」(JST)

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Amylase /ˈæmɪleɪz/ 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

α-Amylase

The α-amylases (EC 3.2.1.1 ) (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)

β-Amylase

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.

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^[5]

γ-Amylase

Gamma-Amylase. Glucan 1,4-alpha-glucosidase

Identifiers

EC number

3.2.1.3

CAS number

9032-08-0

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 / EGO

Search
PMC	articles
PubMed	articles
NCBI	proteins

γ-Amylase (EC 3.2.1.3 ) (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.

Uses

Fermentation

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]

Hyperamylasemia

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]

History

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. Amylase is thought to have played a key role in human evolution in allowing humans an alternative to fruit and protein. A duplication of the pancreatic amylase gene developed independently in humans and rodents, which could be suggestive of the importance of the gene. The salivary amylase levels found in the human lineage are six to eight times higher in humans than in chimpanzees, which are mostly fruit eaters and ingest little starch relative to humans.^[19]

References

^ (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.
^ 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. doi:10.1107/S0907444995014119. PMID 15299664. edit
^ Effects of pH (Introduction to Enzymes)
^ 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. doi:10.1039/c0mb00204f. PMID 21085740. edit
^ "Amylase, Alpha" , I.U.B.: 3.2.1.11,4-α-D-Glucan glucanohydrolase.
^ 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. ISBN 0-13-981176-1.
^ "alpha-Amylase, a flour additive: an important cause of protein contact dermatitis in bakers".
^ "Alpha amylase is a major allergenic component in occupational asthma patients caused by porcine pancreatic extract".
^ 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. PMID 15005645.
^ Mapp CE (May 2001). "Agents, old and new, causing occupational asthma". Occup Environ Med 58 (5): 354–60, 290. doi:10.1136/oem.58.5.354. PMC 1740131. PMID 11303086.
^ http://www.merck.com/mmpe/print/sec02/ch015/ch015b.html
^ "First Biomarker for Human Sleepiness Identified", Record of Washington University in St. Louis, January 25, 2007
^ 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.
^ History of biology 1800–1849
^ 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.
^ Industrial Enzymes for Food Production
^ 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).
^ A History of Fermentation and Enzymes
^ American Scientist. March–April 2010.

External links

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.

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. 血清アミラーゼまたは血清リパーゼの上昇が認められる患者へのアプローチ approach to the patient with elevated serum amylase or lipase
2. 急性膵炎の臨床症状および診断 clinical manifestations and diagnosis of acute pancreatitis
3. 慢性膵炎の治療 treatment of chronic pancreatitis
4. 嚢胞性線維症：膵機能不全の評価およびマネージメント cystic fibrosis assessment and management of pancreatic insufficiency
5. 腎不全患者における血清酵素 serum enzymes in patients with renal failure

English Journal

Vegetable and fermented vegetable juices containing germinated seeds and sprouts of lentil and cowpea.

Simsek S1, El SN1, Kancabas Kilinc A1, Karakaya S2.Author information 1Department of Food Engineering, Faculty of Engineering, Ege University, 35100 İzmir, Turkey.2Department of Food Engineering, Faculty of Engineering, Ege University, 35100 İzmir, Turkey. Electronic address: sibel.karakaya@ege.edu.tr.AbstractHealth-promoting effects of vegetable juice (VJ) and fermented vegetable juice (FVJ) were determined. Both juices displayed antioxidant activity against DPPH radical, and ORAC values obtained for both juices were not statistically different. The α-glucosidase inhibitory activities of the VJ and FVJ were not different. However, α-amylase inhibitory effect of the VJ (IC50: 41μM) was higher than that of FVJ (IC50: 149μM) (p<0.05). In vitro bile acid-binding capacity of FVJ was about 4.30times higher than that of VJ (p<0.05). Although in vitro ACE inhibitory activity of VJ was below 50%, FVJ displayed ACE inhibition (80.2%) with an IC50 value of 50μgprotein/ml. Even though ACE inhibitory activities of digested and undigested FVJ were similar, there was a 42-fold decrease in the IC50 value of FVJ after small intestinal digestion (p<0.05). FVJ, diluted by one half, displayed hemagglutinating activity whilst VJ did not display any hemagglutinating activity.
Food chemistry.Food Chem.2014 Aug 1;156:289-95. doi: 10.1016/j.foodchem.2014.01.095. Epub 2014 Feb 5.
Health-promoting effects of vegetable juice (VJ) and fermented vegetable juice (FVJ) were determined. Both juices displayed antioxidant activity against DPPH radical, and ORAC values obtained for both juices were not statistically different. The α-glucosidase inhibitory activities of the VJ and FVJ
PMID 24629970

Slow glucose release property of enzyme-synthesized highly branched maltodextrins differs among starch sources.

Kittisuban P1, Lee BH2, Suphantharika M3, Hamaker BR4.Author information 1Department of Biotechnology, Faculty of Science, Mahidol University, Rama 6 Road, Bangkok 10400, Thailand; Whistler Center for Carbohydrate Research and Department of Food Science, Purdue University, West Lafayette, IN 47907, USA.2Whistler Center for Carbohydrate Research and Department of Food Science, Purdue University, West Lafayette, IN 47907, USA. Electronic address: lee9@purdue.edu.3Department of Biotechnology, Faculty of Science, Mahidol University, Rama 6 Road, Bangkok 10400, Thailand.4Whistler Center for Carbohydrate Research and Department of Food Science, Purdue University, West Lafayette, IN 47907, USA; Department of Food Science & Technology and Carbohydrate Bioproduct Research Center, Sejong University, 98 Gunja-dong, Gwangjin-gu, Seoul 143-747, Republic of Korea. Electronic address: hamakerb@purdue.edu.AbstractSeven types of starch (waxy corn, normal corn, waxy rice, normal rice, waxy potato, normal potato, and tapioca) were selected to produce slowly digestible maltodextrins by enzymatic modification using a previously developed procedure. Branching enzyme (BE) alone and in combination with β-amylase (BA) were used to increase the amount of α-1,6 branching points, which are slowly hydrolyzed by mucosal α-glucosidases in the small intestine. The enzymatic treatments of all starches resulted in a reduction of the debranched linear chain length distribution and weight-average molecular weight. After α-amylolysis of the enzymatically synthesized-maltodextrins, the proportion of branched α-limit dextrins increased, and consequently a reduction in rate of glucose release by rat intestinal α-glucosidases in vitro. Among the samples, enzyme-modified waxy starches had a more pronounced effect on an increase in the slow digestion property than normal starches. These enzyme-modified maltodextrins show potential as novel functional foods by slowing digestion rate to attain extended glucose release.
Carbohydrate polymers.Carbohydr Polym.2014 Jul 17;107:182-91. doi: 10.1016/j.carbpol.2014.02.033. Epub 2014 Feb 18.
Seven types of starch (waxy corn, normal corn, waxy rice, normal rice, waxy potato, normal potato, and tapioca) were selected to produce slowly digestible maltodextrins by enzymatic modification using a previously developed procedure. Branching enzyme (BE) alone and in combination with β-amylase (B
PMID 24702934

Characteristics of the starch fine structure and pasting properties of waxy rice during storage.

Huang YC1, Lai HM2.Author information 1Department of Agricultural Chemistry, National Taiwan University, No. 1, Roosevelt Rd., Sec. 4, Taipei 10617, Taiwan.2Department of Agricultural Chemistry, National Taiwan University, No. 1, Roosevelt Rd., Sec. 4, Taipei 10617, Taiwan. Electronic address: hmlai@ntu.edu.tw.AbstractTwo waxy rice (TNW1 and TCSW1, exhibiting high and low amylase activity, respectively), were stored at 4 and 17 °C (polished rice) and at room temperature (paddy rice) for 15 months. The fine structure of starch isolated from the aged rice and the pasting properties of starch and rice flour were studied. After storage, the percentage of short amylopectin (AP) chains increased in TNW1, and no uniform changing pattern was observed in the chain-length (CL) distribution of TCSW1. The viscosity of starch isolated from the aged rice increased as the storage temperature and duration increased. We hypothesised that this increase was due to the hydrolysis of AP by endogenous amylase and the generation of small clusters during storage, which caused the simple dissociation of AP and a high swelling degree of starch granules during gelatinisation. Factor analysis of the first two factors associated with the characteristics of viscograms and the CL of AP explained 72% of the total variation.
Food chemistry.Food Chem.2014 Jun 1;152:432-9. doi: 10.1016/j.foodchem.2013.11.144. Epub 2013 Dec 1.
Two waxy rice (TNW1 and TCSW1, exhibiting high and low amylase activity, respectively), were stored at 4 and 17 °C (polished rice) and at room temperature (paddy rice) for 15 months. The fine structure of starch isolated from the aged rice and the pasting properties of starch and rice flour were st
PMID 24444958

Japanese Journal

〔研究ノート〕柿の葉茶浸出液のヒト飲用試験による食後の血糖上昇抑制効果

新海シズ,竹山恵美子,福島正子
學苑 866, 42-46, 2012-12-01
… In our previous study, we found that a persimmon leaf extract solution had an inhibitory effect on -amylase activity, and that although no significant difference was observed, intake of the solution appeared to inhibit blood glucose elevation. …
NAID 110009491052

庭園や美術品の鑑賞による癒しが人の心理や生理に及ぼす効果

内田誠也,岡田雄太,木村友昭 [他]
研究報告集, 31-39, 2012-12
NAID 40019547360

Overexpression of an extraplastidic β-amylase which accumulates in the radish taproot influences the starch content of Arabidopsis thaliana

Takahashi Ikuo,Kuboi Toru,Fujiwara Taketomo [他]
Plant Biotechnology 29(5), 447-455, 2012-12
NAID 40019545212

Related Pictures

★リンクテーブル★

リンク元	「アミラーゼ」
拡張検索	「amylase inhibitor method」

「アミラーゼ」

Beta-Amylase
	Structure of barley beta-amylase. PDB 2xfr
Identifiers
EC number	3.2.1.2
CAS number	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 / EGO
Search
PMC	articles
PubMed	articles
NCBI	proteins

Search
PMC	articles
PubMed	articles
NCBI	proteins

Alpha-Amylase
	Human salivary amylase: calcium ion visible in pale khaki, chloride ion in green. PDB 1SMD
Identifiers
EC number	3.2.1.1
CAS number	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 / EGO
Search
PMC	articles
PubMed	articles
NCBI	proteins

　　[★]

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

「amylase inhibitor method」

　　[★] アミラーゼインヒビター法

[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. doi:10.1107/S0907444995014119. PMID 15299664. edit

[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. doi:10.1039/c0mb00204f. PMID 21085740. edit

[worthington-biochem.com-5] "Amylase, Alpha" , I.U.B.: 3.2.1.11,4-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. ISBN 0-13-981176-1.

[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. PMID 15005645.

[10] Mapp CE (May 2001). "Agents, old and new, causing occupational asthma". Occup Environ Med 58 (5): 354–60, 290. doi:10.1136/oem.58.5.354. PMC 1740131. PMID 11303086.

[11] ttp://www.merck.com/mmpe/print/sec02/ch015/ch015b.html

[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] American Scientist. March–April 2010.

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