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A9228

Sigma-Aldrich

Amyloglucosidase from Rhizopus sp.

≥40,000 units/g solid

Synonym(s):

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

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About This Item

CAS Number:
9032-08-0
Enzyme Commission number:
3.2.1.3 (BRENDA, IUBMB)
EC Number:
232-877-2
MDL number:
MFCD00081350
UNSPSC Code:
12352204
NACRES:
NA.54

form

lyophilized solid

Quality Level

200

specific activity

≥40,000 units/g solid

solubility

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

storage temp.

−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.

Biochem/physiol Actions

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 .

Unit Definition

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

Physical form

Lyophilized salt free powder

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificates of Analysis (COA)

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Daisuke Sugiura et al.
Plant & cell physiology, 58(12), 2043-2056 (2017-12-08)
To clarify whether excessive accumulation of total non-structural carbohydrate (TNC) causes down-regulation of photosynthesis in Raphanus sativus, we manipulated sink-source balance to alter TNC levels in source leaves and examined its effects on photosynthetic characteristics, whole-plant biomass allocation and anatomical
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
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
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
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
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Protocols

Enzymatic Assay of Amyloglucosidase (EC 3.2.1.3)

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

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