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Merck

A9228

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
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-877-2
MDL number:
MFCD00081350
EC Number:
3.2.1.3 (BRENDA, IUBMB)

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Product Name

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

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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A7095A160210115
Amyloglucosidase from Rhizopus sp. ≥40,000 units/g solid

Sigma-Aldrich

A9228

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

Other Notes

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

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].

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

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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Certificates of Analysis (COA)

Lot/Batch Number
0000482398
0000482398
0000456776
0000456728
0000456728

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Daisuke Sugiura et al.
Plant physiology, 183(4), 1600-1611 (2020-06-11)
It has been argued that accumulation of nonstructural carbohydrates triggers a decrease in Rubisco content, which downregulates photosynthesis. However, a decrease in the sink-source ratio in several plant species leads to a decrease in photosynthesis and increases in both structural
Nonawin Lucob-Agustin et al.
Plant science : an international journal of experimental plant biology, 301, 110667-110667 (2020-11-22)
Lateral roots (LRs) are indispensable for plant growth, adaptability and productivity. We previously reported a rice mutant, exhibiting a high density of thick and long LRs (L-type LRs) with long parental roots and herein referred to as promoted lateral root1
Metabolic Control of Fruitbody Morphogenesis in Coprinus cinereus
Gooday GW
Basidium and Basidiocarp, 157-173 (1982)
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
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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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