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1.
J Biomed Opt ; 22(10): 1-10, 2017 Oct.
Article in English | MEDLINE | ID: mdl-29076305

ABSTRACT

A label-free technique for the detection of triacylglycerides by a localized surface plasmon resonance (LSPR)-based biosensor is demonstrated. An LSPR-based fiber-optic sensor probe is fabricated by immobilizing lipase enzyme on silver nanoparticles (Ag-NPs) coated on an unclad segment of a plastic clad optical fiber. The size and shape of nanoparticles were characterized by high-resolution transmission electron microscopy and UV-visible spectroscopy. The peak absorbance wavelength changes with concentration of triacylglycerides surrounding the sensor probe, and sensitivity is estimated from shift in the peak absorbance wavelength as a function of concentration. The fabricated sensor was characterized for the concentration of triacylglyceride solution in the range 0 to 7 mM. The sensor shows the best sensitivity at a temperature of 37°C and pH 7.4 of the triacylglycerides emulsion with a response time of 40 s. A sensitivity of 28.5 nm/mM of triacylglyceride solution is obtained with a limit of detection of 0.016 mM in the entire range of triacylglycerides. This compact biosensor shows good selectivity, stability, and reproducibility in the entire physiological range of triacylglycerides and is well-suited to real-time online monitoring and remote sensing.


Subject(s)
Biosensing Techniques/instrumentation , Fiber Optic Technology , Glycerides/analysis , Metal Nanoparticles/chemistry , Silver/chemistry , Surface Plasmon Resonance , Reproducibility of Results
2.
Biosens Bioelectron ; 79: 693-700, 2016 May 15.
Article in English | MEDLINE | ID: mdl-26773373

ABSTRACT

In this paper, stable, label free enzyme based sensor using long period fiber grating (LPG) is described for the detection of triacylglycerides. A stable covalent binding technique for lipase enzyme immobilization on an optical fiber is reported. An active and stable attachment of the functional group of the enzyme on the fiber surface is achieved using this method. Enzyme immobilization is confirmed by Scanning Electron Microscopy (SEM) and Raman Spectroscopy. The stability is confirmed by lipase p-nitrophenyl palmitate (PNP) assay. In contrast to widely used amperometric based biosensor, where a number of enzymes are required, only one enzyme, namely, lipase is required in our sensor. The sensor shows optimum response within one minute at a temperature of 37°C and pH of 7.4. The sensor is based on the shift in resonance wavelength of the LPG transmission spectrum due to the interaction of triacylglycerides with the enzyme. The biosensor is highly specific towards triacylglycerides and is unaffected by the presence of many other interfering substances in serum. Interaction between the bio-molecules and the long period grating surface is also modeled theoretically using a four layer model for the LPG fiber with the bio-recognition layer and the results obtained are consistent with experimentally obtained results. The sensor shows a high sensitivity of 0.5 nm/mM and a low detection limit of 17.71 mg/dl for the physiological range of triacylglycerides in human blood.


Subject(s)
Biosensing Techniques/instrumentation , Glycerides/blood , Acylation , Biosensing Techniques/methods , Enzymes, Immobilized/chemistry , Enzymes, Immobilized/metabolism , Equipment Design , Glycerides/metabolism , Humans , Limit of Detection , Lipase/chemistry , Lipase/metabolism , Optical Fibers
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