The product has been successfully added to your shopping list.

Glutaminase (Escherichia coli)

Product code: E-GLUTEC

2,500 Units

Prices exclude VAT

Available for shipping

North American customers click here
Content: 2,500 Units
Shipping Temperature: Ambient
Storage Temperature: 2-8oC
Formulation: In 2.5 M lithium sulphate
Physical Form: Suspension
Stability: Minimum 1 year at 4oC. Check vial for details.
Enzyme Activity: Other Activities
EC Number:
CAS Number: 9001-47-2
Synonyms: glutaminase; L-glutamine amidohydrolase
Source: Escherichia coli
Molecular Weight: 33,968
Concentration: Supplied at ~ 1,250 U/mL
Expression: Recombinant from Escherichia coli
Specificity: Catalyses the reaction:
Glutamine + H2O = Glutamate + NH3
Specific Activity: ~ 515 U/mg (25oC, pH 4.9 on L-glutamine)
Unit Definition: One Unit of glutaminase is defined as the amount of enzyme required to deaminate one µmole of L-glutamine (40 mM) to L-glutamate + NH4+ in sodium acetate buffer (40 mM) pH 4.9.
Temperature Optima: 37oC
pH Optima: 4.9
Application examples: Applications for the measurement of glutamine in the food, fermentation and clinical chemistry industries.

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

See our list of analytical enzymes for more products available.

Certificate of Analysis
Safety Data Sheet
FAQs Data Sheet

An L-glutaminase enzyme reactor based on porous bamboo sticks and its application in enzyme inhibitors screening.

Qiao, J., Zhao, L., Liu, L. & Qi, L. (2019). Talanta, 205, 120126.

Inspired by the porous and fibrous structure of commercially available bamboo, herein we created an L-glutaminase enzyme reactor based on bamboo sticks. The enzyme was immobilized onto the bamboo sticks through a glutaraldehyde modification to achieve covalent bonding. The enzymatic hydrolysis efficiency of the prepared L-glutaminase@bamboo sticks based porous enzyme reactor was evaluated by chiral ligand exchange capillary electrochromatography using L-glutamine as the substrate. L-glutaminase@bamboo exhibited improved enzymatic hydrolysis performances, including high hydrolysis efficiency (maximum rate Vmax: two fold higher than the free enzyme), prolonged stability (14 days) and good reusability. L-Glutaminase@bamboo sticks also expanded application capability in pharmaceutical industry in enzyme inhibitor screening. These excellent properties could be attributed to the micropores of bamboo sticks, which led to the fast enzymatic kinetics. The results suggest that the pores of bamboo sticks played an important role in the proposed enzyme reactor during the hydrolysis of L-glutamine and L-glutaminase inhibitor screening.

Hide Abstract
Construction of chiral ligand exchange capillary electrochromatography for D, L-amino acids enantioseparation and its application in glutaminase kinetics study.

Zhao, L., Qiao, J., Zhang, K., Li, D., Zhang, H. & Qi, L. (2018). Journal of Chromatography A, In Press.

A chiral ligand exchange capillary electrochromatography (CLE-CEC) protocol was designed and implemented for D,L-amino acids enantioseparation with poly(maleic anhydride-styrene-methacryloyl-L-arginine methyl ester) as the coating. The block copolymer was synthesized through the reversible addition fragmentation chain transfer reaction. In the constructed CLE-CEC system, poly (methacryloyl-L-arginine methyl ester) moiety of the block copolymer played the role as the immobilized chiral ligand and Zn (II) was used as the central ion. Key factors, including pH of buffer solution, ratio of Zn (II) to ligands, the mass ratio of monomers in the block copolymer, which affect the enantioresolution were investigated. Comparing with the bare capillary, the CLE-CEC enantioresolution was enhanced greatly with the coating one. 5 Pairs of D,L-amino acids enantiomers obtained baseline separation with 5 pairs partly separated. The mechanism of enhancement enantioresolution of the developed CLE-CEC system was explored briefly. Further, good linearities were achieved in the range of 25.0 µM-5.0 mM for quantitative analysis of D-glutamine (r2 = 0.997) and L-glutamine (r2 = 0.991). Moreover, the proposed CLE-CEC assay was successfully applied in the kinetics study of glutaminase by using L-glutamine as the substrate.

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
Guanylate kinase prokaryote E-GMPK
Guanylate kinase (prokaryote)
Glutamate pyruvate transaminase Bacillus subtilis E-GPTBS
Glutamate pyruvate transaminase (Bacillus subtilis)
Glutamate oxaloacetate transaminase Escherichia coli E-GOTEC
Glutamate oxaloacetate transaminase (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)
alpha-Glucosidase yeast maltase E-MALTS
α-Glucosidase (yeast maltase)
Glucose-6-phosphate dehydrogenase Leuconostoc mesenteroides E-GPDH5
Glucose-6-phosphate dehydrogenase (Leuconostoc mesenteroides)