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Glutaminase (Escherichia coli)

Product code: E-GLUTEC

2,500 Units

Prices exclude VAT

This product has been discontinued

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.

This product has been discontinued (read more).

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

Characteristics of a Cold-Adapted L-glutaminase with Potential Applications in the Food Industry.

Ferreira, F. V., Herrmann-Andrade, A. M., Binolfi, A., Calabrese, C. D., Mac Cormack, W. P. & Musumeci, M. A. (2021). Applied Biochemistry and Biotechnology, 1-18.

L-glutaminases are enzymes that catalyze the hydrolysis of L-glutamine, producing L-glutamate and ammonium, and they have promising applications in pharmaceutical and food industries. Several investigations have focused on thermo-tolerant L-glutaminases; however, studies on cold-adapted L-glutaminases have not been reported. These enzymes could be useful in the food industry because they display high catalytic activity at low and room temperatures, a valuable feature in processes aimed to save energy. Besides, they can be easily inactivated by warming and are suitable to prevent decomposition of thermo-labile compounds. The objectives of this work were to characterize the L-glutaminase from the Antarctic bacterium Bizionia argentinensis and analyze its capability as flavor enhancer of protein hydrolysates. The enzyme was heterologously expressed and purified from Escherichia coli, obtaining optimum and homogeneous yields. Kinetic parameters Km and Vmax were located at the lower and upper range of values reported for L-glutaminases, suggesting high catalytic efficiency. Optimum temperature was 25°C, and the enzyme conserved around 90% of maximum activity at 0°C and in presence of 15% (v/v) ethanol and methanol. In saline conditions, the enzyme conserved around 80% of maximum activity in 3 M NaCl. Analysis of structural model suggested cold-adaptation features such as low Arg/(Arg+Lys) ratio and fewer intramolecular interactions than mesophilic and thermo-tolerant L-glutaminases. This work provides a novel cold-adapted L-glutaminase with promising features in the food industry.

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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.

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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.

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Safety Information
Symbol : Not Applicable
Signal Word : Not Applicable
Hazard Statements : Not Applicable
Precautionary Statements : Not Applicable
Safety Data Sheet
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