49291
Glucosidase from Aspergillus niger
powder, ≥750 U/g
Synonym(s):
Cellobiase
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About This Item
Specific activity:
≥750 U/g
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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.
Other Notes
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
Characterization; Ethanol production from paper-mill waste fibre
Characterizationcitationcitation; Ethanol production from paper-mill waste fibrecitation
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
Regulatory Information
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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
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
Xia, Z. et al.
Enzyme and Microbial Technology, 15, 62-62 (1993)
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
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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