A9228
Amyloglucosidase from Rhizopus sp.
≥40,000 units/g solid
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form
lyophilized solid
Quality Level
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
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
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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
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
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
Protocols
This procedure may be used for the determination of Amyloglucosidase activity using starch as the substrate.
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