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Safety Information

49291

Sigma-Aldrich

Glucosidase from Aspergillus niger

powder, ≥750 U/g

Synonym(s):

Cellobiase

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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

form

powder

Quality Level

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

Pictograms

Health hazard

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

Regulatory Information

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McCleary, B.V., and Harrington, J.,
Methods in Enzymology, 160, 575-575 (1988)
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
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)
Xia, Z. et al.
Enzyme and Microbial Technology, 15, 62-62 (1993)

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