49291
Glucosidase from Aspergillus niger
powder, ≥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
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
常规特殊物品
Certificates of Analysis (COA)
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Chunmei Wu et al.
Carbohydrate polymers, 250, 116985-116985 (2020-10-15)
In this study, citric acid (CA) esterified canna starch was firstly synthesized with the aid of vacuum, microwave and infrared radiation treatment. The changes in structural, physicochemical properties and in vitro digestibility of the modified starch were then investigated. The
Xiaohong Lan et al.
Food chemistry, 188, 632-640 (2015-06-05)
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
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)
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
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