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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/10/22 17:22:49」(JST)

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Sucrase is the name given to a number of enzymes that catalyze the hydrolysis of sucrose to fructose and glucose. The enzyme invertase, which occurs more commonly in plants, also hydrolyzes sucrose but by a different mechanism.^[1]

Types

EC 3.2.1.10 is sucrase-isomaltase
EC 3.2.1.26 is invertase
EC 3.2.1.48

Physiology

Sucrose intolerance (also known as Congenital Sucrase-Isomaltase Deficiency (CSID) or Sucrase-isomaltase deficiency) occurs when sucrase is not secreted in the small intestine. With sucrose intolerance, the result of consuming sucrose is excess gas production and often diarrhea and malabsorption. Lactose intolerance is a related disorder that reflects an individual's inability to hydrolyze the disaccharide lactose.

Sucrase is secreted by the tips of the villi of the epithelium in the small intestine. Its levels are reduced in response to villi-blunting events such as celiac sprue and the inflammation associated with the disorder. The levels increase in Pregnancy/Lactation and Diabetes as the villi hypertrophy.

Use in chemical analysis

Sucrose itself is a non-reducing sugar and therefore will not test positive with Benedict's solution. In order to test for sucrose, the sample is treated with sucrase. The sucrose is hydrolysed into glucose and fructose, with glucose being a reducing sugar, which in turn tests positive with Benedict's solution^{[citation needed]}.

References

^ Hubert Schiweck, Margaret Clarke, Günter Pollach "Sugar” in Ullmann’s Encyclopedia of Industrial Chemistry 2007, Wiley-VCH, Weinheim. doi:10.1002/14356007.a25_345.pub2

External links

Sucrase at the US National Library of Medicine Medical Subject Headings (MeSH)
Diagnosis of sucrase deficiency

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UpToDate Contents

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1. 糖尿病の治療におけるα-グルコシダーゼ阻害剤およびリパーゼ阻害剤 alpha glucosidase inhibitors and lipase inhibitors for treatment of diabetes mellitus
2. グリコーゲン脱分枝酵素欠損症（糖原病III型） glycogen debrancher deficiency glycogen storage disease iii
3. 2型糖尿病における持続性高血糖のマネージメント management of persistent hyperglycemia in type 2 diabetes mellitus
4. 2型糖尿病の予防 prevention of type 2 diabetes mellitus
5. 成人における過敏性腸症候群の治療 treatment of irritable bowel syndrome in adults

English Journal

Fermentation in the small intestine contributes substantially to intestinal starch disappearance in calves.

Gilbert MS1, Pantophlet AJ2, Berends H3, Pluschke AM4, van den Borne JJ3, Hendriks WH3, Schols HA5, Gerrits WJ3.
The Journal of nutrition.J Nutr.2015 Jun;145(6):1147-55. doi: 10.3945/jn.114.208595. Epub 2015 Apr 15.
BACKGROUND: The proportion of starch disappearing from the small intestinal lumen is generally lower in ruminants than in monogastric animals, and there are indications that the starch digestion capacity in ruminants is limited.OBJECTIVES: Milk-fed calves were used to study the rate-limiting enzyme
PMID 25878206

Structural elements responsible for the glucosidic linkage-selectivity of a glycoside hydrolase family 13 exo-glucosidase.

Saburi W1, Rachi-Otsuka H1, Hondoh H2, Okuyama M1, Mori H1, Kimura A3.
FEBS letters.FEBS Lett.2015 Mar 24;589(7):865-9. doi: 10.1016/j.febslet.2015.02.023. Epub 2015 Feb 26.
Glycoside hydrolase family 13 contains exo-glucosidases specific for α-(1→4)- and α-(1→6)-linkages including α-glucosidase, oligo-1,6-glucosidase, and dextran glucosidase. The α-(1→6)-linkage selectivity of Streptococcus mutans dextran glucosidase was altered to α-(1→4)-linkage selectiv
PMID 25728274

Old meets new: identifying founder mutations in genetic disease.

Evans JA1.
CMAJ : Canadian Medical Association journal = journal de l'Association medicale canadienne.CMAJ.2015 Feb 3;187(2):93-4. doi: 10.1503/cmaj.141509. Epub 2015 Jan 19.
PMID 25602001

Japanese Journal

Saccharomyces cerevisiae 由来oligo-1,6-glucosidaseの基質認識機構について

山本惠三,三宅英雄,楠木正巳,大崎茂芳
Journal of Applied Glycoscience Supplement 2010(0), 77-77, 2010
NAID 130004626960

Molecular Cloning and Characterization of an Enzyme Hydrolyzing p-Nitrophenyl α-D-Glucoside from Bacillus stearothermophilus SA0301

Kobayashi Atsushi,Tonozuka Takashi,Sato Kimihiko [他],SUYAMA Mikita,SASAKI Jun,NYAMDAWAA Batbold,SAKAGUCHI Masayoshi,SAKANO Yoshiyuki
Bioscience, biotechnology, and biochemistry 70(2), 495-499, 2006-02-23
… SA0301 produces an extracellular oligo-1,6-glucosidase (bsO16G) that also hydrolyzes p-nitrophenyl α-D-glucoside (Tonozuka et al., J. … values of bsO16G for isomaltotriose and isomaltose were 13.2 and 1.39 s−1·mM−1 …
NAID 10018534552

Arthrobacter globiformis I42 由来 oligo-1,6-glucosidase 遺伝子の単離, 発現および組換え酵素の諸性質

山口幸三,森本奈保喜,王一,渡辺賢二,海野剛裕,伊藤浩之,松井博和
Journal of applied glycoscience 51(1), 37-40, 2004-01-20
NAID 10012483880

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