form
lyophilized powder
specific activity
≥20 units/mg solid
storage temp.
−20°C
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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
存储类别
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
法规信息
新产品
此项目有
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.
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
Anthony Guiseppi-Elie
Analytical and bioanalytical chemistry, 399(1), 403-419 (2010-10-22)
Following hemorrhage-causing injury, lactate levels rise and correlate with the severity of injury and are a surrogate of oxygen debt. Posttraumatic injury also includes hyperglycemia, with continuously elevated glucose levels leading to extensive tissue damage, septicemia, and multiple organ dysfunction
Zafar Hussain Ibupoto et al.
Sensors (Basel, Switzerland), 12(3), 2456-2466 (2012-06-28)
In this work, fabrication of gold coated glass substrate, growth of ZnO nanorods and potentiometric response of lactic acid are explained. The biosensor was developed by immobilizing the lactate oxidase on the ZnO nanorods in combination with glutaraldehyde as a
A Poscia et al.
Biosensors & bioelectronics, 20(11), 2244-2250 (2005-03-31)
A novel continuous lactate monitoring system has been developed modifying the GlucoDay portable medical device (A. Menarini Diagnostics), already present in the European market, and used to continuously measure glucose levels. Lactate oxidase based biosensors have been developed immobilising the
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