{"product_id":"l-glutamate-oxidase-from-streptomyces-sp","title":"L-Glutamate Oxidase from Streptomyces sp.","description":"\u003cdiv style=\"max-width:1400px; margin:0 auto; padding:40px 20px; font-family:'Open Sans',sans-serif; font-weight:300; background:#fff; color:#333; font-size:0.95rem; box-sizing:border-box;\"\u003e\n  \u003cdiv style=\"display:flex; flex-direction:column; gap:20px;\"\u003e\n    \u003ch2 style=\"margin:0; font-weight:600;\"\u003eL-Glutamate Oxidase from Streptomyces sp. – Catalog #B2025913\u003c\/h2\u003e\n    \u003cp\u003e\n      L-Glutamate Oxidase from \u003cem\u003eStreptomyces\u003c\/em\u003e sp. (Catalog #B2025913) is a high-purity enzyme supplied as 1 unit of lyophilized powder. \n      This oxidoreductase catalyzes the oxidative deamination of L-glutamate to α-ketoglutarate, ammonia, and hydrogen peroxide. \n      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.\n    \u003c\/p\u003e\n    \n    \u003c!-- SPEC TABLE --\u003e\n    \u003cdiv style=\"overflow-x:auto; max-width:100%; margin-bottom:20px;\"\u003e\n      \u003ctable style=\"width:500px; border-collapse:collapse;\"\u003e\n        \u003ctbody\u003e\n          \u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n            \u003ctd style=\"width:150px; padding-right:10px;\"\u003e\u003cstrong\u003eCatalog number:\u003c\/strong\u003e\u003c\/td\u003e\n            \u003ctd\u003eB2025913\u003c\/td\u003e\n          \u003c\/tr\u003e\n          \u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n            \u003ctd style=\"width:150px; padding-right:10px;\"\u003e\u003cstrong\u003eLot number:\u003c\/strong\u003e\u003c\/td\u003e\n            \u003ctd\u003eBatch Dependent\u003c\/td\u003e\n          \u003c\/tr\u003e\n          \u003ctr style=\"border-bottom:1px solid:#ddd;\"\u003e\n            \u003ctd style=\"width:150px; padding-right:10px;\"\u003e\u003cstrong\u003eExpiration Date:\u003c\/strong\u003e\u003c\/td\u003e\n            \u003ctd\u003eBatch dependent\u003c\/td\u003e\n          \u003c\/tr\u003e\n          \u003ctr style=\"border-bottom:1px solid:#ddd;\"\u003e\n            \u003ctd style=\"width:150px; padding-right:10px;\"\u003e\u003cstrong\u003eAmount:\u003c\/strong\u003e\u003c\/td\u003e\n            \u003ctd\u003e1 unit\u003c\/td\u003e\n          \u003c\/tr\u003e\n          \u003ctr style=\"border-bottom:1px solid:#ddd;\"\u003e\n            \u003ctd style=\"width:150px; padding-right:10px;\"\u003e\u003cstrong\u003eMolecular Weight or Concentration:\u003c\/strong\u003e\u003c\/td\u003e\n            \u003ctd\u003eN\/A\u003c\/td\u003e\n          \u003c\/tr\u003e\n          \u003ctr style=\"border-bottom:1px solid:#ddd;\"\u003e\n            \u003ctd style=\"width:150px; padding-right:10px;\"\u003e\u003cstrong\u003eSupplied as:\u003c\/strong\u003e\u003c\/td\u003e\n            \u003ctd\u003eLyophilized Powder\u003c\/td\u003e\n          \u003c\/tr\u003e\n          \u003ctr style=\"border-bottom:1px solid:#ddd;\"\u003e\n            \u003ctd style=\"width:150px; padding-right:10px;\"\u003e\u003cstrong\u003eApplications:\u003c\/strong\u003e\u003c\/td\u003e\n            \u003ctd\u003eGlutamate quantification assays, glutamate biosensors, food industry analysis, neuroscience research, clinical diagnostics, and enzymatic bioprocessing\u003c\/td\u003e\n          \u003c\/tr\u003e\n          \u003ctr style=\"border-bottom:1px solid:#ddd;\"\u003e\n            \u003ctd style=\"width:150px; padding-right:10px;\"\u003e\u003cstrong\u003eStorage:\u003c\/strong\u003e\u003c\/td\u003e\n            \u003ctd\u003e2-8°C\u003c\/td\u003e\n          \u003c\/tr\u003e\n          \u003ctr style=\"border-bottom:1px solid:#ddd;\"\u003e\n            \u003ctd style=\"width:150px; padding-right:10px;\"\u003e\u003cstrong\u003eKeywords:\u003c\/strong\u003e\u003c\/td\u003e\n            \u003ctd\u003eL-Glutamate Dehydrogenase, Glutamate Oxidase, Glutamate Aminotransferase, L-Glutamate-oxidizing enzyme, Streptomyces Glutamate Oxidase, Streptomyces sp. Glutamate Oxidase\u003c\/td\u003e\n          \u003c\/tr\u003e\n          \u003ctr style=\"border-bottom:1px solid:#ddd;\"\u003e\n            \u003ctd style=\"width:150px; padding-right:10px;\"\u003e\u003cstrong\u003eGrade:\u003c\/strong\u003e\u003c\/td\u003e\n            \u003ctd\u003eBiotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity \u0026gt;18 MΩ-cm) and are filtered through 0.22 um.\u003c\/td\u003e\n          \u003c\/tr\u003e\n        \u003c\/tbody\u003e\n      \u003c\/table\u003e\n    \u003c\/div\u003e\n    \n    \u003c!-- SCIENTIFIC OVERVIEW --\u003e\n    \u003ch3 style=\"margin-top:30px;\"\u003eScientific Overview\u003c\/h3\u003e\n    \u003cp\u003e\n      L-Glutamate Oxidase is a flavin-dependent oxidoreductase that catalyzes the reaction: L-glutamate + O₂ + H₂O → α-ketoglutarate + NH₃ + H₂O₂. \n      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. \n      Its high specificity and the generation of hydrogen peroxide make it an excellent coupling enzyme for colorimetric or electrochemical detection systems.\n    \u003c\/p\u003e\n    \u003cp\u003e\n      Key applications include:\n    \u003c\/p\u003e\n    \u003cul style=\"padding-left:20px;\"\u003e\n      \u003cli\u003eGlutamate biosensors and real-time monitoring\u003c\/li\u003e\n      \u003cli\u003eEnzymatic quantification of L-glutamate in food and beverages\u003c\/li\u003e\n      \u003cli\u003eNeuroscience research (neurotransmitter analysis)\u003c\/li\u003e\n      \u003cli\u003eClinical diagnostics and metabolic studies\u003c\/li\u003e\n      \u003cli\u003eBiocatalysis and bioprocessing\u003c\/li\u003e\n    \u003c\/ul\u003e\n    \n    \u003c!-- USAGE \u0026 HANDLING --\u003e\n    \u003ch3 style=\"margin-top:30px;\"\u003eUsage \u0026amp; Handling Guidance\u003c\/h3\u003e\n    \u003cp\u003e\n      Store the lyophilized powder at 2–8°C. Reconstitute in sterile ultrapure water or appropriate buffer to the desired activity concentration. \n      Prepare single-use aliquots to maintain stability. The enzyme is typically used in coupled assays with peroxidase for colorimetric or fluorometric detection of H₂O₂.\n    \u003c\/p\u003e\n    \u003cul style=\"padding-left:20px;\"\u003e\n      \u003cli\u003e\n\u003cstrong\u003eRecommended working concentration:\u003c\/strong\u003e 0.1–1 U\/mL (optimize for specific assay)\u003c\/li\u003e\n      \u003cli\u003e\n\u003cstrong\u003eStability:\u003c\/strong\u003e Lyophilized form is stable at 2–8°C; reconstituted solutions should be used promptly or stored frozen\u003c\/li\u003e\n      \u003cli\u003e\n\u003cstrong\u003eReaction conditions:\u003c\/strong\u003e Typically pH 7.0–8.0, 25–37°C\u003c\/li\u003e\n    \u003c\/ul\u003e\n    \n    \u003c!-- WHAT YOU GET --\u003e\n    \u003ch3 style=\"margin-top:30px;\"\u003eWhat You Get\u003c\/h3\u003e\n    \u003cul style=\"padding-left:20px;\"\u003e\n      \u003cli\u003e1 unit of L-Glutamate Oxidase from \u003cem\u003eStreptomyces\u003c\/em\u003e sp. as lyophilized powder\u003c\/li\u003e\n      \u003cli\u003eHigh-purity biotechnology-grade enzyme with strong specificity for L-glutamate\u003c\/li\u003e\n      \u003cli\u003eConvenient quantity for assay development and small-scale research\u003c\/li\u003e\n      \u003cli\u003eFor research use only (RUO)\u003c\/li\u003e\n    \u003c\/ul\u003e\n    \n    \u003c!-- WHY RESEARCHERS CHOOSE IT --\u003e\n    \u003ch3 style=\"margin-top:30px;\"\u003eWhy Researchers Choose It\u003c\/h3\u003e\n    \u003cul style=\"padding-left:20px;\"\u003e\n      \u003cli\u003eHigh specificity for L-glutamate with reliable H₂O₂ production\u003c\/li\u003e\n      \u003cli\u003eExcellent for glutamate biosensors and enzymatic assays\u003c\/li\u003e\n      \u003cli\u003eStable lyophilized format suitable for long-term storage\u003c\/li\u003e\n      \u003cli\u003eProven performance in food analysis, neuroscience, and clinical research\u003c\/li\u003e\n      \u003cli\u003eBiotechnology-grade purity with consistent activity\u003c\/li\u003e\n    \u003c\/ul\u003e\n    \n    \u003c!-- FAQ --\u003e\n    \u003ch3 style=\"margin-top:30px;\"\u003eFrequently Asked Questions (FAQ)\u003c\/h3\u003e\n    \u003cul style=\"padding-left:20px;\"\u003e\n      \u003cli\u003e\n\u003cstrong\u003eWhat reaction does L-Glutamate Oxidase catalyze?\u003c\/strong\u003e\u003cbr\u003e\n        L-Glutamate + O₂ + H₂O → α-ketoglutarate + NH₃ + H₂O₂.\u003c\/li\u003e\n      \u003cli\u003e\n\u003cstrong\u003eWhat is the primary application of this enzyme?\u003c\/strong\u003e\u003cbr\u003e\n        It is widely used in glutamate biosensors and enzymatic assays for quantitative determination of L-glutamate.\u003c\/li\u003e\n      \u003cli\u003e\n\u003cstrong\u003eHow should I reconstitute the enzyme?\u003c\/strong\u003e\u003cbr\u003e\n        Dissolve in sterile ultrapure water or buffer to the desired concentration. Aliquot and store appropriately.\u003c\/li\u003e\n      \u003cli\u003e\n\u003cstrong\u003eWhat storage conditions are recommended?\u003c\/strong\u003e\u003cbr\u003e\n        Store lyophilized powder at 2–8°C.\u003c\/li\u003e\n      \u003cli\u003e\n\u003cstrong\u003eIs this enzyme suitable for food industry use?\u003c\/strong\u003e\u003cbr\u003e\n        Yes. It is commonly employed for glutamate quantification in food and beverage analysis.\u003c\/li\u003e\n    \u003c\/ul\u003e\n    \n    \u003cdiv style=\"margin-top:20px; font-weight:bold; color:#c8102e;\"\u003e\n      This product is for Research Use Only (RUO). It is not intended for diagnostic or therapeutic use in humans or animals.\n    \u003c\/div\u003e\n    \n    \u003chr\u003e\n    \n   \u003ch4\u003eReferences\u003c\/h4\u003e\n\n\u003cul style=\"padding-left: 0; margin: 0; list-style: none;\"\u003e\n\n  \u003cli style=\"display: flex; justify-content: space-between; align-items: flex-start; gap: 12px; padding: 8px 0; border-bottom: 1px solid #eee;\"\u003e\n    \u003cspan style=\"flex: 1;\"\u003e\n      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 \u003cem\u003eStreptomyces\u003c\/em\u003e sp. X-119-6.\n      \u003cem\u003eJ Biochem.\u003c\/em\u003e 2003 Dec;134(6):805-12.\n    \u003c\/span\u003e\n    \u003ca href=\"https:\/\/doi.org\/10.1093\/jb\/mvg206\" target=\"_blank\" style=\"flex-shrink: 0; margin-top: 2px;\"\u003e\n      \u003cimg src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/Reference.png?v=1775409336\" alt=\"Reference\" style=\"height: 28px; width: auto;\"\u003e\n    \u003c\/a\u003e\n  \u003c\/li\u003e\n\n  \u003cli style=\"display: flex; justify-content: space-between; align-items: flex-start; gap: 12px; padding: 8px 0; border-bottom: 1px solid #eee;\"\u003e\n    \u003cspan style=\"flex: 1;\"\u003e\n      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 \u003cem\u003eStreptomyces\u003c\/em\u003e sp. X-119-6.\n      \u003cem\u003eFEBS J.\u003c\/em\u003e 2009 Jul;276(14):3894-903.\n    \u003c\/span\u003e\n    \u003ca href=\"https:\/\/doi.org\/10.1111\/j.1742-4658.2009.07103.x\" target=\"_blank\" style=\"flex-shrink: 0; margin-top: 2px;\"\u003e\n      \u003cimg src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/Reference.png?v=1775409336\" alt=\"Reference\" style=\"height: 28px; width: auto;\"\u003e\n    \u003c\/a\u003e\n  \u003c\/li\u003e\n\n  \u003cli style=\"display: flex; justify-content: space-between; align-items: flex-start; gap: 12px; padding: 8px 0; border-bottom: 1px solid #eee;\"\u003e\n    \u003cspan style=\"flex: 1;\"\u003e\n      Utsumi T, Arima J, Sakaguchi C, Tamura T, Sasaki C, Kusakabe H, Sugio S, Inagaki K. Arg305 of \u003cem\u003eStreptomyces\u003c\/em\u003e L-glutamate oxidase plays a crucial role for substrate recognition.\n      \u003cem\u003eBiochem Biophys Res Commun.\u003c\/em\u003e 2012 Jan 20;417(3):951-5.\n    \u003c\/span\u003e\n    \u003ca href=\"https:\/\/doi.org\/10.1016\/j.bbrc.2011.12.033\" target=\"_blank\" style=\"flex-shrink: 0; margin-top: 2px;\"\u003e\n      \u003cimg src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/Reference.png?v=1775409336\" alt=\"Reference\" style=\"height: 28px; width: auto;\"\u003e\n    \u003c\/a\u003e\n  \u003c\/li\u003e\n\n  \u003cli style=\"display: flex; justify-content: space-between; align-items: flex-start; gap: 12px; padding: 8px 0; border-bottom: 1px solid #eee;\"\u003e\n    \u003cspan style=\"flex: 1;\"\u003e\n      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.\n      \u003cem\u003eSens Actuators B Chem.\u003c\/em\u003e 2006;119(2):570-576.\n    \u003c\/span\u003e\n    \u003ca href=\"https:\/\/doi.org\/10.1016\/j.snb.2006.01.008\" target=\"_blank\" style=\"flex-shrink: 0; margin-top: 2px;\"\u003e\n      \u003cimg src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/Reference.png?v=1775409336\" alt=\"Reference\" style=\"height: 28px; width: auto;\"\u003e\n    \u003c\/a\u003e\n  \u003c\/li\u003e\n\n  \u003cli style=\"display: flex; justify-content: space-between; align-items: flex-start; gap: 12px; padding: 8px 0; border-bottom: 1px solid #eee;\"\u003e\n    \u003cspan style=\"flex: 1;\"\u003e\n      Wang L, Peng R, Tian Y, Liu M, Yao Q. Isolation and characterization of a novel L-glutamate oxidase with strict substrate specificity from \u003cem\u003eStreptomyces diastatochromogenes\u003c\/em\u003e.\n      \u003cem\u003eBiotechnol Lett.\u003c\/em\u003e 2017 Apr;39(4):523-528.\n    \u003c\/span\u003e\n    \u003ca href=\"https:\/\/doi.org\/10.1007\/s10529-016-2269-y\" target=\"_blank\" style=\"flex-shrink: 0; margin-top: 2px;\"\u003e\n      \u003cimg src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/Reference.png?v=1775409336\" alt=\"Reference\" style=\"height: 28px; width: auto;\"\u003e\n    \u003c\/a\u003e\n  \u003c\/li\u003e\n\n  \u003cli style=\"display: flex; justify-content: space-between; align-items: flex-start; gap: 12px; padding: 8px 0; border-bottom: 1px solid #eee;\"\u003e\n    \u003cspan style=\"flex: 1;\"\u003e\n      Niu P, Dong X, Wang Y, Liu L. Enzymatic production of α-ketoglutaric acid from L-glutamic acid via L-glutamate oxidase.\n      \u003cem\u003eJ Biotechnol.\u003c\/em\u003e 2014;179:56-62.\n    \u003c\/span\u003e\n    \u003ca href=\"https:\/\/doi.org\/10.1016\/j.jbiotec.2014.03.021\" target=\"_blank\" style=\"flex-shrink: 0; margin-top: 2px;\"\u003e\n      \u003cimg src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/Reference.png?v=1775409336\" alt=\"Reference\" style=\"height: 28px; width: auto;\"\u003e\n    \u003c\/a\u003e\n  \u003c\/li\u003e\n\n  \u003cli style=\"display: flex; justify-content: space-between; align-items: flex-start; gap: 12px; padding: 8px 0; border-bottom: 1px solid #eee;\"\u003e\n    \u003cspan style=\"flex: 1;\"\u003e\n      Yano Y, Matsuo S, Ito N, Tamura T, Kusakabe H, Inagaki K, Imada K. A new L-arginine oxidase engineered from L-glutamate oxidase.\n      \u003cem\u003eProtein Sci.\u003c\/em\u003e 2021 May;30(5):1044-1055.\n    \u003c\/span\u003e\n    \u003ca href=\"https:\/\/doi.org\/10.1002\/pro.4070\" target=\"_blank\" style=\"flex-shrink: 0; margin-top: 2px;\"\u003e\n      \u003cimg src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/Reference.png?v=1775409336\" alt=\"Reference\" style=\"height: 28px; width: auto;\"\u003e\n    \u003c\/a\u003e\n  \u003c\/li\u003e\n\n  \u003cli style=\"display: flex; justify-content: space-between; align-items: flex-start; gap: 12px; padding: 8px 0; border-bottom: 1px solid #eee;\"\u003e\n    \u003cspan style=\"flex: 1;\"\u003e\n      Pollegioni L, Motta P, Molla G. L-amino acid oxidase as biocatalyst: a dream too far?\n      \u003cem\u003eAppl Microbiol Biotechnol.\u003c\/em\u003e 2013 Nov;97(21):9323-41.\n    \u003c\/span\u003e\n    \u003ca href=\"https:\/\/doi.org\/10.1007\/s00253-013-5230-1\" target=\"_blank\" style=\"flex-shrink: 0; margin-top: 2px;\"\u003e\n      \u003cimg src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/Reference.png?v=1775409336\" alt=\"Reference\" style=\"height: 28px; width: auto;\"\u003e\n    \u003c\/a\u003e\n  \u003c\/li\u003e\n\n  \u003cli style=\"display: flex; justify-content: space-between; align-items: flex-start; gap: 12px; padding: 8px 0; border-bottom: 1px solid #eee;\"\u003e\n    \u003cspan style=\"flex: 1;\"\u003e\n      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 \u003cem\u003eStreptomyces\u003c\/em\u003e sp. X119-6 with catalase (KatE) to whole-cell systems for glutaric acid production in \u003cem\u003eEscherichia coli\u003c\/em\u003e.\n      \u003cem\u003eKorean J Chem Eng.\u003c\/em\u003e 2021;38:2106-2112.\n    \u003c\/span\u003e\n    \u003ca href=\"https:\/\/doi.org\/10.1007\/s11814-021-0855-8\" target=\"_blank\" style=\"flex-shrink: 0; margin-top: 2px;\"\u003e\n      \u003cimg src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/Reference.png?v=1775409336\" alt=\"Reference\" style=\"height: 28px; width: auto;\"\u003e\n    \u003c\/a\u003e\n  \u003c\/li\u003e\n\n  \u003cli style=\"display: flex; justify-content: space-between; align-items: flex-start; gap: 12px; padding: 8px 0; border-bottom: 1px solid #eee;\"\u003e\n    \u003cspan style=\"flex: 1;\"\u003e\n      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.\n      \u003cem\u003eEnzyme Microb Technol.\u003c\/em\u003e 2020;136:109530.\n    \u003c\/span\u003e\n    \u003ca href=\"https:\/\/doi.org\/10.1016\/j.enzmictec.2020.109530\" target=\"_blank\" style=\"flex-shrink: 0; margin-top: 2px;\"\u003e\n      \u003cimg src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/Reference.png?v=1775409336\" alt=\"Reference\" style=\"height: 28px; width: auto;\"\u003e\n    \u003c\/a\u003e\n  \u003c\/li\u003e\n\n\u003c\/ul\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e","brand":"Molecular Depot","offers":[{"title":"Default Title","offer_id":51607852187946,"sku":"BTS-B2025913","price":795.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/B2025913-600x537.png?v=1780083395","url":"https:\/\/bluetigerscientific.com\/products\/l-glutamate-oxidase-from-streptomyces-sp","provider":"Blue Tiger Scientific","version":"1.0","type":"link"}