EC Number   |
Application |
Reference |
|---|
   1.1.3.2 | analysis |
development of a bienzyme fiberoptic sensor for flow injection analysis of L-lactate using lactate oxidase and peroxidase immobilized on a polyamide membrane. Hydrogen peroxide generated by lactate oxidase is substrate of peroxidase in presence of luminol. For the sensor strip, the detection limit is 250 pmol lactate, with 1.7% variation for 10 replicates using 6.25 nmol lactate |
744805 |
| 1.1.3.2 | analysis |
engineering the enzyme in order to minimize the effects of oxygen interference on sensor strips. Mutant A96L shows a drastic reduction in oxidase activity using molecular oxygen as the electron acceptor and a small increase in dehydrogenase activity employing an artificial electron acceptor. After immobilization on a screen-printed carbon electrode and under argon or atmospheric conditions, the response current increases linearly from 0.05 to 0.5 mM L-lactate for both wild-type and mutant A96L. Under atmospheric conditions, the response of wild-type electrode is suppressed by 9-12% due to oxygen interference. The mutant maintains 56-69% of the response current at the same L-lactate level and minimizes the relative bias error to -19% from -49% of wild-type |
744533 |
| 1.1.3.2 | biotechnology |
coupling of mutant S218C in 94% yield to maleimide-activated methoxypoly(ethylene glycol) 5000. PEGylation causes about 30% small decrease in the specific activity of the S218C mutant, and it does not change the protein stability |
744446 |
| 1.1.3.2 | diagnostics |
an improved amperometric L-lactate biosensor was constructed based on covalent immobilization of lactate oxidase from Pediococcus species onto carboxylated multiwalled carbon nanotubes (cMWCNT)/copper nanoparticles (CuNPs)/polyaniline (PANI) hybrid film electrodeposited on the surface of a pencil graphite electrode. The biosensor shows maximum response within 5 s at pH 8.0 in 0.05 M sodium phosphate buffer and 37°C, when operated at 20 mV/s. The biosensor has a detection limit of 0.00025 mM with a wide working range between 0.001-2.5 mM. The biosensor is employed for measurement of L-lactic acid level in plasma of apparently healthy and diseased persons. Analytical recovery of added lactic acid in plasma is 95.5%. The working enzyme electrode is used 180 times over a period of 140 days, when stored at 4°C |
762991 |
| 1.1.3.2 | diagnostics |
an integrated tear lactate sensor using Schirmer test strip and engineered lactate oxidase is developed. The sensor is insensitive to ascorbic acid, acetaminophen, and uric acid, which are common interfering compounds in tears, and show no sign of degradation after 8 weeks of shelf life study. The proposed sensor exhibits potential usefulness in providing an alternative noninvasive method of measuring lactate and in calibrating the continuous lactate contact lens |
763746 |
| 1.1.3.2 | diagnostics |
L-lactate oxidase based lactate sensors are widely used for clinical diagnostics, sports medicine, and food quality control. Rational engineering of Aerococcus viridans L-lactate oxidase for the mediator modification to achieve quasi-direct electron transfer type lactate sensor |
-, 762835 |
| 1.1.3.2 | food industry |
L-lactate oxidase based lactate sensors are widely used for clinical diagnostics, sports medicine, and food quality control. Rational engineering of Aerococcus viridans L-lactate oxidase for the mediator modification to achieve quasi-direct electron transfer type lactate sensor |
-, 762835 |
| 1.1.3.2 | medicine |
L-lactate oxidase based lactate sensors are widely used for clinical diagnostics, sports medicine, and food quality control. Rational engineering of Aerococcus viridans L-lactate oxidase for the mediator modification to achieve quasi-direct electron transfer type lactate sensor |
-, 762835 |
| 1.1.3.2 | synthesis |
biocascade synthesis of L-tyrosine derivatives by coupling a thermophilic tyrosine phenol-lyase and L-lactate oxidase. o-Phenol derivatives are transformed into the corresponding L-tyrosine derivatives with excellent stereoselectivity and high yields using an efficient one-pot, two-step cascade containing thermophilic tyrosine phenol-lyase mutants from Symbiobacterium toebii and L-lactate oxidase from Aerococcus viridans |
-, 763001 |
| 1.1.3.2 | synthesis |
enzymatic preparation of pyruvate by a whole-cell biocatalyst coexpressing L-lactate oxidase and catalase. Under the optimized transformation conditions, pyruvate is produced at a titer of 59.9 g/l and a yield of 90.8% in a substrate fed-batch process, promising an alternative route for the green production of pyruvate |
763662 |
