L-Glutamate Oxidase from Streptomyces sp. – Catalog #B2025913

L-Glutamate Oxidase from Streptomyces sp. (Catalog #B2025913) is a high-purity enzyme supplied as 1 unit of lyophilized powder. This oxidoreductase catalyzes the oxidative deamination of L-glutamate to α-ketoglutarate, ammonia, and hydrogen peroxide. It is widely used in glutamate biosensors, enzymatic assays for L-glutamate quantification in food, cell culture, and neuroscience research, as well as in clinical diagnostics and bioprocessing applications.

Scientific Overview

L-Glutamate Oxidase is a flavin-dependent oxidoreductase that catalyzes the reaction: L-glutamate + O₂ + H₂O → α-ketoglutarate + NH₃ + H₂O₂. The enzyme is widely utilized in amperometric biosensors for real-time glutamate monitoring in neuroscience and clinical diagnostics, as well as in enzymatic assays for glutamate determination in food products and cell culture media. Its high specificity and the generation of hydrogen peroxide make it an excellent coupling enzyme for colorimetric or electrochemical detection systems.

Key applications include:

• Glutamate biosensors and real-time monitoring
• Enzymatic quantification of L-glutamate in food and beverages
• Neuroscience research (neurotransmitter analysis)
• Clinical diagnostics and metabolic studies
• Biocatalysis and bioprocessing

Usage & Handling Guidance

Store the lyophilized powder at 2–8°C. Reconstitute in sterile ultrapure water or appropriate buffer to the desired activity concentration. Prepare single-use aliquots to maintain stability. The enzyme is typically used in coupled assays with peroxidase for colorimetric or fluorometric detection of H₂O₂.

• Recommended working concentration: 0.1–1 U/mL (optimize for specific assay)
• Stability: Lyophilized form is stable at 2–8°C; reconstituted solutions should be used promptly or stored frozen
• Reaction conditions: Typically pH 7.0–8.0, 25–37°C

What You Get

• 1 unit of L-Glutamate Oxidase from Streptomyces sp. as lyophilized powder
• High-purity biotechnology-grade enzyme with strong specificity for L-glutamate
• Convenient quantity for assay development and small-scale research
• For research use only (RUO)

Why Researchers Choose It

• High specificity for L-glutamate with reliable H₂O₂ production
• Excellent for glutamate biosensors and enzymatic assays
• Stable lyophilized format suitable for long-term storage
• Proven performance in food analysis, neuroscience, and clinical research
• Biotechnology-grade purity with consistent activity

Frequently Asked Questions (FAQ)

• What reaction does L-Glutamate Oxidase catalyze?
  L-Glutamate + O₂ + H₂O → α-ketoglutarate + NH₃ + H₂O₂.
• What is the primary application of this enzyme?
  It is widely used in glutamate biosensors and enzymatic assays for quantitative determination of L-glutamate.
• How should I reconstitute the enzyme?
  Dissolve in sterile ultrapure water or buffer to the desired concentration. Aliquot and store appropriately.
• What storage conditions are recommended?
  Store lyophilized powder at 2–8°C.
• Is this enzyme suitable for food industry use?
  Yes. It is commonly employed for glutamate quantification in food and beverage analysis.

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References

• Arima J, Tamura T, Kusakabe H, Ashiuchi M, Yagi T, Tanaka H, Inagaki K. Recombinant expression, biochemical characterization and stabilization through proteolysis of an L-glutamate oxidase from Streptomyces sp. X-119-6. J Biochem. 2003 Dec;134(6):805-12.
• Arima J, Sasaki C, Sakaguchi C, Mizuno H, Tamura T, Kashima A, Kusakabe H, Sugio S, Inagaki K. Structural characterization of L-glutamate oxidase from Streptomyces sp. X-119-6. FEBS J. 2009 Jul;276(14):3894-903.
• Utsumi T, Arima J, Sakaguchi C, Tamura T, Sasaki C, Kusakabe H, Sugio S, Inagaki K. Arg305 of Streptomyces L-glutamate oxidase plays a crucial role for substrate recognition. Biochem Biophys Res Commun. 2012 Jan 20;417(3):951-5.
• Upadhyay S, Ohgami N, Kusakabe H, Mizuno H, Arima J, Tamura T, Inagaki K, Suzuki H. Performance characterization of recombinant L-glutamate oxidase in a micro GOT/GPT sensing system. Sens Actuators B Chem. 2006;119(2):570-576.
• Wang L, Peng R, Tian Y, Liu M, Yao Q. Isolation and characterization of a novel L-glutamate oxidase with strict substrate specificity from Streptomyces diastatochromogenes. Biotechnol Lett. 2017 Apr;39(4):523-528.
• Niu P, Dong X, Wang Y, Liu L. Enzymatic production of α-ketoglutaric acid from L-glutamic acid via L-glutamate oxidase. J Biotechnol. 2014;179:56-62.
• Yano Y, Matsuo S, Ito N, Tamura T, Kusakabe H, Inagaki K, Imada K. A new L-arginine oxidase engineered from L-glutamate oxidase. Protein Sci. 2021 May;30(5):1044-1055.
• Pollegioni L, Motta P, Molla G. L-amino acid oxidase as biocatalyst: a dream too far? Appl Microbiol Biotechnol. 2013 Nov;97(21):9323-41.
• Ham S, Han YH, Kim SH, Suh MJ, Cho JY, Lee HJ, Park SH, Park K, Ahn J, Joo JC, Bhatia SK, Yang YH. Application of L-glutamate oxidase from Streptomyces sp. X119-6 with catalase (KatE) to whole-cell systems for glutaric acid production in Escherichia coli. Korean J Chem Eng. 2021;38:2106-2112.
• Zhang X, Xu N, Li J, Ma Z, Wei L, Liu Q, Liu J. Engineering of L-glutamate oxidase as the whole-cell biocatalyst for the improvement of α-ketoglutarate production. Enzyme Microb Technol. 2020;136:109530.