A2330
Amyloglucosidase from Candida tsukubaensis
ammonium sulfate suspension, 50-150 units/mg protein
Synonym(s):
1,4-α-D-Glucan glucohydrolase, Exo-1,4-α-glucosidase, Glucoamylase
form
ammonium sulfate suspension
specific activity
50-150 units/mg protein
storage temp.
2-8°C
Application
These enzymes are widely used in the manufacture of glucose and fructose syrup, as well as in industrial saccharification.
Biochem/physiol Actions
Glucoamylases are originally of fungal origin usually occurring in multiple forms. Glucoamylase catalyze the hydrolysis of α-1,4 and α-1,6 glucosidic linkages to release β-D glucose from non-reducing ends of starch and non-related poly- and oligosaccharides. Glucoamylase is capable of converting starch completely to glucose. The enzymes of this group effect a hydrolysis of starch by a single chain mechanism in which glucose units are removed from the nonreducing end of a linear chain until complete hydrolysis of the chain has been effected. Hydrolyzes the α-D-(1→4) glucosidic linkages in starch and maltooligosaccharides. Amyloglucosidase is capable of hydrolyzing the α-D-(1→4), the α-D-(1→6) and the α-D-(1→3) glucosidic bonds of oligosaccharide.
Physical form
Suspension in 3.2 M (NH4)2SO4, pH approx. 5.5.
Other Notes
One unit will liberate 1.0 mg of glucose from starch in 3 min at pH 4.5 at 55 °C.
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
Storage Class
12 - Non Combustible Liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type ABEK (EN14387) respirator filter
Regulatory Information
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The Action of an Amyloglucosidase of Aspergillus niger on Starch and Malto-oligosaccharides
John H. Pazur & Tadahiko Ando
The Journal of Biological Chemistry, 234(8), 65-75 null
H. Kamal
J. Macromol. Sci. Chem., 45, 65-75 (2008)
R De Mot et al.
Antonie van Leeuwenhoek, 51(3), 275-287 (1985-01-01)
The starch-degrading yeast Candida tsukubaensis CBS 6389 secreted amylase at high activity when grown in a medium containing soluble starch. The extracellular alpha-amylase activity was very low. The major amylase component was purified by DEAE-Sephadex A-50 chromatography and Ultrogel AcA
The action of an amyloglucosidase of Aspergillus niger on starch and malto-oligosaccharides.
J H PAZUR et al.
The Journal of biological chemistry, 234(8), 1966-1970 (1959-08-01)
Juan Antonio Tamayo-Ramos et al.
Biotechnology and bioengineering, 110(2), 543-551 (2012-09-06)
In filamentous fungi, most of the strategies used for the improvement of protein yields have been based on an increase in the transcript levels of a target gene. Strategies focusing at the translational level have been also described, but are
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