Dehydrogenase based reagentless biosensor for monitoring phenylketonuria

Weiss, David J.; Dorris, Megan K.; Loh, Amanda; Peterson, Laura E.

doi:10.1016/j.bios.2006.09.001

Cited by 51 publications

(38 citation statements)

References 26 publications

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“…In the work reported here, the FEED technique was applied to the enzyme-linked amperometric immuno-sensing scheme and the feasibility of using this new detection approach as a biomarker detection technique was demonstrated by the detection of the biomarker CA 125, using electrodes modified with carbon nanotube. The incorporation of the two detection methods has resulted in a reagentless assay approach (Wang, 2005;Weiss et al, 2007), another advantage of the reported technique, which does not use electron transfer mediators and the substrate of the enzyme used to label the secondary antibody. As the result of the signal amplification, the detection limit of the detection system was lowered from 4.9 U/ml to 0.9 U/ml.…”

Section: Introductionmentioning

confidence: 99%

Field-effect amperometric immuno-detection of protein biomarker

Wang

Yau

2011

Biosensors and Bioelectronics

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Section: Introductionmentioning

confidence: 99%

Field-effect amperometric immuno-detection of protein biomarker

Wang

Yau

2011

Biosensors and Bioelectronics

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“…Weiss and coworkers prepared and characterized the first reagentless dehydrogenase based biosensor for monitoring Phe levels in human urine with a Phe detection limit of 0.5 mM [2]. More recently, a PKU screening method based on gas chromatography-mass spectrometry (GC-MS) and tandem mass spectrometry (MS-MS) was developed.…”

Section: Introductionmentioning

confidence: 98%

“…The main symptom of PKU is the accumulation of Phe in blood, urine, and cerebrospinal fluid. The clinical ranges of Phe for patients in human blood and urine are 0.6~3.8 and 20~60 mM, respectively [2].…”

Section: Introductionmentioning

confidence: 99%

Application of a quartz crystal nanobalance to the molecularly imprinted recognition of phenylalanine in solution

Mirmohseni

Shojaei

Farbodi

2008

Biotechnol Bioproc E

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A quartz crystal nanobalance (QCN) biosensor was developed for the selective determination of phenylalanine (Phe) in aqueous solutions. A Phe imprinted copolymer was synthesized using polyacrylonitrile and acrylic acid [poly(AN-co-AA)]. The copolymer was then coated on quartz crystal electrode to form complementary structures for the template recognition of Phe. The composite electrode was then used to determine Phe levels in solution. Determinations were based on frequency shifts of molecularly imprinted polymer (MIP) modified quartz crystal electrode caused by Phe adsorption. The frequency shifts were linearly dependent on Phe concentration over the range 50~500 mgL −1 . The results obtained show that the imprinted poly(AN-co-AA) modified biosensor had higher sensitivity (0.5839 Hz/mgL −1 ) than a non-molecularly imprinted copolymer (0.2724 Hz/mgL −1 ). Furthermore, good reproducibility, R.S.D. = 1.84% (n = 7) was observed, and the detection limit was 45 mgL −1 . The selectivity of the imprinted poly(AN-co-AA) modified biosensor was examined using a number of analytes similar to Phe,=áKÉK, dopamine (DA), ascorbic acid (AscA), vanillylmandelic acid (VMA), uric acid (UA), tryptophan (Trp), and tyrosine (Tyr), and the results obtained showed a size dependent selective effect. © KSBB hÉóïçêÇëW=éÜÉåóä~ä~åáåÉI=ÄáçëÉåëçêI=èì~êíò=Åêóëí~ä=å~åçÄ~ä~åÅÉI=éçäóE^kJÅçJ^^FI=jfm= = = = =

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“…In order to increase its stability and economical application, special attention is currently devoted on the modification and the immobilization of L-PheDH. For instance, L-PheDH immobilization on tresylated poly(vinyl alcohol) beads [16], modification with cyclodextrin derivatives [17], biosensor coated amino-activated cellulose membrane by cross-linking with glutaraldehyde (GDA) [18], L-adamantanyl modified L-PheDH immobilization on β-cyclodextrins coated Au electrode [19], and carbon paste electrode with 3,4-dihydroxybenzaldehyde as an electron mediator [20] can be given as examples to the limited research in this area.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Phenylalanine Dehydrogenase and Its Application in Flow-Injection Analysis System for Determination of Plasma Phenylalanine

Tarhan

Ayar-Kayali

2010

Appl Biochem Biotechnol

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Phenylalanine dehydrogenase (L-PheDH) from Sporosarcina ureae was immobilized on DEAE-cellulose, modified initially with 2-amino-4,6-dichloro-s-triazine followed by hexamethylenediamine and glutaraldehyde. The highest activity of immobilized PheDH was determined as 95.75 U/g support with 56% retained activity. The optimum pH value of immobilized L-PheDH was shifted from pH 10.4 to 11.0. The immobilized L-PheDH showed activity variations close to the maximum value in a wider temperature range of 45-55 °C, whereas it was 40 °C for the native enzyme. The pH and the thermal stability of the immobilized L-PheDH were also better than the native enzyme. At pH 10.4 and 25 °C, K (m) values of the native and the immobilized L-PheDH were determined as K(m Phe) = 0.118, 0.063 mM and K(m NAD)(+) = 0.234, 0.128 mM, respectively. Formed NADH at the exit of packed bed reactor column was detected by the flow-injection analysis system. The conversion efficiency of the reactor was found to be 100% in the range of 5-600 μM Phe at 9 mM NAD(+) with a total flow rate of 0.1 mL/min. The reactor was used for the analyses of 30 samples each for 3 h per day. The half-life period of the reactor was 15 days.

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Dehydrogenase based reagentless biosensor for monitoring phenylketonuria

Cited by 51 publications

References 26 publications

Field-effect amperometric immuno-detection of protein biomarker

Field-effect amperometric immuno-detection of protein biomarker

Application of a quartz crystal nanobalance to the molecularly imprinted recognition of phenylalanine in solution

Immobilization of Phenylalanine Dehydrogenase and Its Application in Flow-Injection Analysis System for Determination of Plasma Phenylalanine

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