L0638
Lactate Oxidase from Pediococcus sp.
lyophilized powder, ≥20 units/mg solid
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About This Item
CAS Number:
UNSPSC Code:
12352204
EC Number:
232-841-6
MDL number:
Specific activity:
≥20 units/mg solid
form
lyophilized powder
specific activity
≥20 units/mg solid
storage temp.
−20°C
General description
Formerly E.C. number 1.1.3.2
Lactate oxidase is a globular flavoprotein and utilizes flavin mononucleotide (FMN) as the cofactor. The enzyme contains a major tyrosine in the substrate-binding pocket and a flavin adenine dinucleotide (FAD) active site. Lactate oxidase has several bacterial sources.
Application
Lactate Oxidase from Pediococcus sp. has been:
- used to functionalize the detection reservoirs for lactate analysis
- used in sequential enzymatic reactions to measure lactate production in the supernatants of microglial cultures
- immobilized onto a carbon electrode to generate a self-powered lactate sensor
Biochem/physiol Actions
Lactate oxidase is used in immobilization or enzyme-based labels for designing biochemical analytical devices such as immunosensors. This enzyme catalyzes the oxidation of lactate to produce pyruvate and H2O2. Lactate oxidase is useful in the first-generation biosensor approach for the electrochemical detection of lactate.
Other Notes
One unit will oxidize 1.0 μmole of L-lactate to pyruvate and H2O2 per min at pH 6.5 at 37 °C.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
Regulatory Information
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Thomas Stoisser et al.
Scientific reports, 6, 27892-27892 (2016-06-16)
L-Lactate oxidase (LOX) belongs to a large family of flavoenzymes that catalyze oxidation of α-hydroxy acids. How in these enzymes the protein structure controls reactivity presents an important but elusive problem. LOX contains a prominent tyrosine in the substrate binding
Ying Chen et al.
Biosensors & bioelectronics, 29(1), 115-118 (2011-08-30)
Detection of analytes in complex biological samples, such as milk and blood, normally requires sample pretreatment. These pretreatment regimes reduce assay throughput and increase testing costs. Technologies that make it possible to eliminate sample pretreatment are of great industrial interest.
Jacob M Goran et al.
Analytical chemistry, 83(21), 8123-8129 (2011-09-29)
Nitrogen-doped carbon nanotubes (N-CNTs) provide a simple, robust, and unique platform for biosensing. Their catalytic activity toward the oxygen reduction reaction (ORR) and subsequent hydrogen peroxide (H(2)O(2)) disproportionation creates a sensitive electrochemical response to enzymatically generated H(2)O(2) on the N-CNT
Marcelo Ricardo Romero et al.
Analytical chemistry, 82(13), 5568-5572 (2010-06-04)
An amperometric sensor for lactate quantification is presented. The developed biosensor requires only 0.2 U of lactate oxidase, which is immobilized in a mucin/albumin hydrogel matrix. By protecting the platinum surface with a Nafion membrane, typical interference related to negatively
Parvin Samadi Pakchin et al.
Biosensors & bioelectronics, 122, 68-74 (2018-09-23)
In this work, a novel simple and sensitive electrochemical immunosensor was developed based on lactate oxidase as a single electrochemical probe for the detection of carcinoma antigen 125 (CA125). Chitosan-gold nanoparticle/multiwall carbon nanotube/graphene oxide (CS-AuNP/MWCNT/GO) was used as the electrode
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