The product has been successfully added to your shopping list.

β-Glucuronidase (Escherichia coli)

Product code: E-BGLAEC

500,000 Units

Prices exclude VAT

Available for shipping

North American customers click here
Content: 500,000 Units
Shipping Temperature: Ambient
Storage Temperature: 2-8oC
Formulation: In solution (Tris.HCl/NaCl/EDTA)
Physical Form: Solution
Stability: > 4 years at 4oC
Enzyme Activity: β-Glucuronidase
EC Number:
CAZy Family: GH2
CAS Number: 9001-45-0
Synonyms: β-D-glucuronoside glucuronosohydrolase; GUS
Source: Escherichia coli
Molecular Weight: 82,600
Concentration: Supplied at ~ 250 kU/mL
Expression: Recombinant from Escherichia coli
Specificity: Hydrolysis of non-reducing terminal β-D-glucuronic acid residues from glycoproteins and oligosaccharides of glycoconjugates.
Specific Activity: ~ 15,000 U/mg (37oC, pH 6.8 on phenolphthalein-β-D-glucuronide);
~ 50 U/mg (37oC, pH 7.5 on pNP-β-D-glucuronide)
Unit Definition: 30000 U/mg protein: One Unit of β-D-glucuronosidase activity is defined as the amount of enzyme required to release one µg of phenolphthalein per hour from phenolphthalein-β-D-glucuronide (0.5 mM) in sodium phosphate buffer (100 mM) at pH 6.8 and 37oC.
110 U/mg protein: One Unit of β-D-glucuronosidase activity is defined as the amount of enzyme required to release one µmole of p-nitrophenol per minute from pNP-β-D-glucuronide (1 mM) in Tris.HCl buffer (100 mM) pH 7.5 and 37oC., monitored at 410 nm.
Temperature Optima: 37oC
pH Optima: 6.8

High purity recombinant β-Glucuronidase (Escherichia coli) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

Do Not Freeze/Thaw.

Looking for other enzymes? Browse our Carbohydrate Active enZYme and glycobiology enzyme products lists.

Certificate of Analysis
Safety Data Sheet
Data Sheet
Effect of heat-moisture treatment on multi-scale structures and physicochemical properties of breadfruit starch.

Tan, X., Li, X., Chen, L., Xie, F., Li, L. & Huang, J. (2017). Carbohydrate Polymers, 161, 286-294.

Breadfruit starch was subjected to heat-moisture treatment (HMT) at different moisture content (MC). HMT did not apparently change the starch granule morphology but decreased the molecular weight and increased the amylose content. With increased MC, HMT transformed the crystalline structure (B → A + B → A) and decreased the relative crystallinity. With ≥25% MC, the scattering peak at ca. 0.6 nm−1 disappeared, suggesting the lamellar structure was damaged. Compared with native starch, HMT-modified samples showed greater thermostability. Increased MC contributed to a higher pasting temperature, lower viscosity, and no breakdown. The pasting temperature of native and HMT samples ranged from 68.8 to 86.2&‌deg;C. HMT increased the slowly-digestible starch (SDS) and resistant starch (RS) contents. The SDS content was 13.24% with 35% MC, which was 10.25% higher than that of native starch. The increased enzyme resistance could be ascribed to the rearrangement of molecular chains and more compact granule structure.

Hide Abstract
Safety Information
Symbol : Not Applicable
Signal Word : Not Applicable
Hazard Statements : Not Applicable
Precautionary Statements : Not Applicable
Safety Data Sheet
Customers also viewed
beta-Glucosidase Phanerochaete chrysosporium E-BGOSPC
β-Glucosidase (Phanerochaete chrysosporium)
beta-Glucosidase Agrobacterium sp E-BGOSAG
β-Glucosidase (Agrobacterium sp.)
Pectate Lyase Aspergillus sp E-PCLYAN
Pectate Lyase (Aspergillus sp.)
Hexokinase yeast E-HEX10
Hexokinase (yeast)
Glutaminase Escherichia coli E-GLUTEC
Glutaminase (Escherichia coli)
alpha-Glucuronidase Geobacillus stearothermophilus E-AGUBS
α-Glucuronidase (Geobacillus stearothermophilus)
beta-Glucosidase Thermotoga maritima E-BGOSTM
β-Glucosidase (Thermotoga maritima)
beta-Glucosidase Aspergillus niger E-BGLUC
β-Glucosidase (Aspergillus niger)