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A9228

Amyloglucosidase from Rhizopus sp.

≥40,000 units/g solid

Synonym(e):

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

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1 G

€ 938,00

10 G

€ 5.140,00

€ 938,00

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Über diesen Artikel

CAS-Nummer:
9032-08-0
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-877-2
MDL number:
MFCD00081350
EG-Nummer:
3.2.1.3 (BRENDA, IUBMB)
Specific activity:
≥40,000 units/g solid

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Unterstützung erhalten

form

lyophilized solid

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

Quality Level

200

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Amyloglucosidase from Rhizopus sp. ≥40,000 units/g solid

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Amyloglucosidase from Rhizopus sp.

Amyloglucosidase from Aspergillus niger ≥260 U/mL, aqueous solution

Sigma-Aldrich

A7095

Amyloglucosidase from Aspergillus niger

Amyloglucosidase from Aspergillus niger ammonium sulfate suspension, ≥40 units/mg protein

Sigma-Aldrich

A1602

Amyloglucosidase from Aspergillus niger

Amyloglucosidase from Aspergillus niger lyophilized, powder, ~70 U/mg

Sigma-Aldrich

10115

Amyloglucosidase from Aspergillus niger

specific activity

≥40,000 units/g solid

specific activity

≥260 U/mL

specific activity

≥40 units/mg protein

specific activity

~70 U/mg

form

lyophilized solid

form

aqueous solution

form

ammonium sulfate suspension

form

powder

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

solubility

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

solubility

-

solubility

-

solubility

-

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

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).[1] The enzyme has been used in the glycosylation of N-vanillyl-nonanamide to form a water-soluble component with pharmacological applications.[2] The glycogen was estimated in stipe residue of Coprinus cinereus by treating with amyloglucosidase and measuring the amount of glucose produced.[3]

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 [4].

Physical form

Lyophilized salt free powder

Other Notes

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

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Lagerklasse

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Analysenzertifikate (COA)

Lot/Batch Number
0000531357
0000531357
0000513909
0000513909
0000482398

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In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

Metabolic Control of Fruitbody Morphogenesis in Coprinus cinereus
Gooday GW
Basidium and Basidiocarp, 157-173 (1982)
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
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
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Protokolle

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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