49291
Glucosidase from Aspergillus niger
powder, gray-brown, ≥750 U/g
Synonym(s):
Cellobiase
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Biochem/physiol Actions
Glucosidase catalyzes the hydrolysis of α-1,4 linkages with a substrate preference for maltose, maltotriose and maltotetraose. Reactivity with large polysaccharides like dextrin and starch have also been described.
Glucosidase catalyzes the hydrolysis of α-1,4 linkages with a substrate preference for maltose, maltotriose and maltotetraose. Reactivity with large polysaccharides like dextrin and starch have also been described.
Unit Definition
1 U corresponds to the amount of enzyme which hydrolyzes 1 μmol p-nitrophenyl-β-D-glucopyranoside per minute at pH 4.0 and 37 °C; may contain α- and β-glucosidase
Other Notes
Characterization; Ethanol production from paper-mill waste fibre
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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T Watanabe et al.
European journal of biochemistry, 209(2), 651-659 (1992-10-15)
Beta-glucosidase was purified from a crude cellulase preparation from Aspergillus niger by affinity chromatography on a methacrylamide-N-methylene-bis-methacrylamide copolymer bearing cellobiamine. The purified enzyme was a dimer with an isoelectric point of 4.0. The molecular mass of the enzyme was estimated
McCleary, B.V., and Harrington, J.,
Methods in Enzymology, 160, 575-575 (1988)
Action of α-D-glucosidase from Aspergillus niger towards dextrin and starch
M. Ota et al
Carbohydrate Polymers, 78, 287-291 (2009)
Substrate specificity and subsite affinities of crystalline α-glucosidase from Aspergillus niger
A. Kita et al
Agricultural and Biological Chemistry, 55, 2327-2335 (1991)
J H Pazur et al.
Carbohydrate research, 58(1), 193-202 (1977-09-01)
The action patterns of glucoamylase (amyloglucosidase) and glucosyltransferase (transglucosylase) on D-[1-14C]glucose, [1-14C]maltose, and [1-14C]malto-oligosaccharides (labeled at position 1 of the D-glucose group at the reducing end) have been investigated by paper-chromatographic and oligosaccharide-mapping techniques. Under the conditions of the experiments
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