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Key Documents

A9228

Sigma-Aldrich

Amyloglucosidase from Rhizopus sp.

≥40,000 units/g solid

Synonyme(s) :

1,4-α-D-Glucan glucohydrolase, Exo-1,4-α-glucosidase, Glucoamylase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Forme

lyophilized solid

Activité spécifique

≥40,000 units/g solid

Solubilité

0.03 M sodium citrate-phosphate buffer, pH 4.5: soluble 5.0 mg/mL

Température de stockage

−20°C

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Application

Amyloglucosidase is used to hydrolyze α-D-glucosides. It may be used in the brewing of beer and in the production of bread and juices. Amyloglucosidase, from Rhizopus sp., has been used to study the cleavage of oligosaccharides during ER-associated degradation of proteins (ERAD). The enzyme has been used in the glycosylation of N-vanillyl-nonanamide to form a water-soluble component with pharmacological applications. The glycogen was estimated in stipe residue of Coprinus cinereus by treating with amyloglucosidase and measuring the amount of glucose produced.

Actions biochimiques/physiologiques

Amyloglucosidases are capable of hydrolyzing the α-D-(1-4), the α-D-(1-6), and the α-D-(1-3) glucosidic bonds of oligosaccharides .

Définition de l'unité

One unit will liberate 1.0 mg of glucose from starch in 3 min at pH 4.5 at 55 °C.

Forme physique

Lyophilized salt free powder

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

Masabumi Komatsu et al.
Physiologia plantarum, 147(2), 159-168 (2012-05-23)
To determine the effects of elevated CO(2) concentration ([CO(2)]) on the temperature-dependent photosynthetic properties, we measured gas exchange and chlorophyll fluorescence at various leaf temperatures (15, 20, 25, 30, 35 and 40°C) in 1-year-old seedlings of the Japanese white birch
Ramaiah Sivakumar et al.
Biotechnology letters, 29(10), 1537-1548 (2007-07-05)
Enzymatic syntheses of N-vanillyl-nonanamide, 1, glycosides with D-glucose, 2, D-galactose, 3, D-mannose, 4, D-ribose, 5, maltose, 6, and lactose, 7, were carried out using amyloglucosidase from Rhizopus and beta-glucosidase from sweet almond. The latter catalysed the syntheses of N-vanillyl-nonanamide glycosides
Daisuke Sugiura et al.
Annals of botany, 123(4), 715-726 (2018-12-06)
Sink-source imbalance could cause an accumulation of total non-structural carbohydrates (TNC; soluble sugar and starch) in source leaves. We aimed to clarify interspecific differences in how sink-source imbalance and TNC causes the downregulation of photosynthesis among three legume plants. The
Isabelle Chantret et al.
The Journal of biological chemistry, 286(48), 41786-41800 (2011-10-08)
In Saccharomyces cerevisiae, proteins with misfolded lumenal, membrane, and cytoplasmic domains are cleared from the endoplasmic reticulum (ER) by ER-associated degradation (ERAD)-L, -M, and -C, respectively. ERAD-L is N-glycan-dependent and is characterized by ER mannosidase (Mns1p) and ER mannosidase-like protein
Metabolic Control of Fruitbody Morphogenesis in Coprinus cinereus
Gooday GW
Basidium and Basidiocarp, 157-173 (1982)

Protocoles

This procedure may be used for the determination of Amyloglucosidase activity using starch as the substrate.

This procedure may be used for the determination of Amyloglucosidase activity using starch as the substrate.

This procedure may be used for the determination of Amyloglucosidase activity using starch as the substrate.

This procedure may be used for the determination of Amyloglucosidase activity using starch as the substrate.

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