49291
Glucosidase from Aspergillus niger
powder, ≥750 U/g
Synonym(s):
Cellobiase
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About This Item
Recommended Products
form
powder
specific activity
≥750 U/g
storage temp.
2-8°C
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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
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
Certificates of Analysis (COA)
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Action of α-D-glucosidase from Aspergillus niger towards dextrin and starch
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Substrate specificity and subsite affinities of crystalline α-glucosidase from Aspergillus niger
Agricultural and Biological Chemistry, 55, 2327-2335 (1991)
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
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Starches from five underutilized tubers (canna, potato, Chinese yam, water chestnut, and taro) were extracted to investigate quantitative structure-property relationships (QSPR) in each starch using a combination of X-ray diffraction (XRD) and small-angle X-ray scattering (SAXS). Structural parameters of the
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