University of North Florida
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Stuart Chalk, Ph.D.
Department of Chemistry
University of North Florida
Phone: 1-904-620-1938
Fax: 1-904-620-3535
Email: schalk@unf.edu
Website: @unf

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l-Lysine

  • IUPAC Name: (2S)-2,6-diaminohexanoic acid
  • Molecular Formula: C6H14N2O2
  • CAS Registry Number: 56-87-1
  • InChI: InChI=1S/C6H14N2O2/c7-4-2-1-3-5(8)6(9)10/h5H,1-4,7-8H2,(H,9,10)/t5-/m0/s1
  • InChI Key: KDXKERNSBIXSRK-YFKPBYRVSA-N

@ ChemSpider@ NIST@ PubChem

Citations 8

"Development Of An Interferent Free Amperometric Biosensor For Determination Of L-lysine In Food"
Anal. Chim. Acta 2000 Volume 412, Issue 1-2 Pages 111-119
S. C. Kelly, P. J. O'Connell, C. K. O'Sullivan and G. G. Guilbault

Abstract: A highly selective, fast responding amperometric biosensor is described, useful for the determination of L-lysine in food. Common electrochemical interferences, like acetoaminophen and ascorbic acid have zero response at +100 mV applied onto a ruthenium/rhodium coated glassy carbon electrode covered with 1,2-diaminobenzene polymer. This novel transducer was coupled with L-lysine α-oxidase purified from Trichoderma viride and at the appropriate pH, classic substrate interferences from L-ornithine, L-arginine and L-phenylalanine are reduced to 3.4, 1.1 and 0.7% of the response to L-lysine (taken as 100%). No other amino acids respond. The sensor is inexpensive to produce, has excellent repeatability and very good reproducibility. Thus, the L-lysine (protein) content of foods can be almost specifically determined following rapid microwave digestion of the product.
Food Amperometry Sensor Electrode Sample preparation Interferences Detector

"Enzymatic Determination Of L-lysine By Flow Injection Techniques"
Anal. Chim. Acta 1990 Volume 235, Issue 1-3 Pages 329-335
Andreas Pohlmann and Wolfgang W. Stamm, Hitoshi Kusakabe, Maria-Regina Kula

Abstract: Samples (2 µL) were injected into a carrier stream (~0.8 mL min-1) of 0.2 M phosphate buffer (pH 7.4) and mixed with a reagent stream containing phenol and 4-aminoantipyrine. The mixture was passed through an enzyme reactor. The enzyme reactor consisted of a perspex cartridge (4 cm x 3 mm) filled with 100 mg of VA-Epoxy Biosynth resin on which L-lysine oxidase and horse-radish peroxidase were co-immobilized. The color development in the stream was monitored at 500 nm. Response was rectilinear for up to 16 mM L-lysine with an injection volume of 2 µL; the detection limit was 1 mM but could be improved to 0.05 mM by increasing the injection volume to 36 µL. Analysis time was 30 samples h-1. The technique could also be used with both enzymes in solution or with L-lysine oxidase immobilized and horse-radish peroxidase in solution
Enzyme Buffer pH Resin Immobilized enzyme Detection limit

"Chemiluminometric L-lysine Determination With Immobilized Lysine Oxidase By Flow Injection Analysis"
Anal. Chim. Acta 1993 Volume 280, Issue 2 Pages 185-189
F. Preuschoff and U. Spohn*, E. Weber, K. Unverhau, K. -H. Mohr

Abstract: L-Lysine oxidase (5 mg) and BSA (15 mg) in 1-2 mL of 0.1 M phosphate buffer of pH 6.5 were immobilized onto 200 mg of aminosilylated Bioran glass (190-200 µm; Schott, Mainz, Germany) which had been activated with 2.5% glutaraldehyde in 0.1 M phosphate buffer of pH 6.5 for 1 h and packed into a Plexiglas tube (1.5 cm x 2 mm i.d.). Peroxidase (7 mg in 200 µL of phosphate buffer) was immobilized onto an Ultrabind membrane (Gelman Sciences, Ann Arbor, MI, USA) and incorporated into a chemiluminescent H2O2 sensor (Fresenius' J. Anal. Chem., 1993, in press). Samples were injected into 0.1 M potassium phosphate buffer of pH 7.4. The H2O2 produced by lysine oxidase was carried in 33 mM carbonate buffer of pH 10.4 containing 0.677 mM luminol to the H2O2 sensor. The sensor flow-rate was 0.5 ml/min and the pH was 8.5; the signal was transferred via a fiber-optic bundle to a photomultiplier. The calibration graph was linear from 10 µM to 1 mM L-lysine with a detection limit of 5 µM; no RSD are given. The sampling rate was 90/h and the stability was >1 month. Ascorbic acid and some amino-acids interfered. Interference by bivalent Co, Fe and Ni was suppressed with EDTA.
Chemiluminescence Immobilized enzyme Interferences

"Flow Injection Amperometric Biosensor Based On Immobilized L-lysine-α-oxidase For L-lysine Determination"
Anal. Lett. 1994 Volume 27, Issue 15 Pages 2849-2860
Simonian, A.L.;Badalian, I.E.;Berezov, T.T.;Smirnova, I.P.;Khaduev, S.H.

Abstract: Silica gel was modified by Robinsons method and lysine oxidase was covalently linked to the silica gel by continuous stirring for 4 h at 10°C. The resulting silica gel was washed with 50 mM potassium phosphate buffer of pH 8.2 and put into a mini reactor (11 cm x 4 mm i.d.). The minireactor was installed in a FIA system (block diagram given). A 50 mM phosphate buffer solution of pH 8 was pumped using a peristaltic pump at 400 ml/h through the system. A sample (70 µL) was injected into the buffer stream, through the minireactor for detection by a Clark O2 electrode. The calibration graph was linear up to 5.5 mM L-lysine with a detection limit of 0.2 mM. The specificity of the assay is tabulated.
Biological Amperometry Sensor Immobilized enzyme Silica gel

"Selective Biosensing Of L-lysine By A Low-temperature Flow Injection Technique Using An Immobilized Lysine Oxidase Reactor"
Anal. Sci. 1996 Volume 12, Issue 1 Pages 87-90
R. L. C. CHEN, M.-H. LEE and K. MATSUMOTO

Abstract: A method for the determination of L-lysine (lysine; I) using a H2O2 electrode as a biosensor device in an enzymatic FIA system is presented and used to analyze the concentration of I in fish feed. Squid or white-fish meal (10 g) was suspended in 100 mL 0.1 M phosphate buffer of pH 7.3 (buffer A) and the suspension was incubated with protease (10 000 U Denazyme AP) for a definite time. The reaction mixtures were incubated at 90°C for 10 min and centrifuged at 11 000 g for 1 h. The supernatants were filtered (0.45 µm) and a 20 µL portion of the filtrate was injected into a carrier stream of buffer A (3 ml/min) of an automated flow injection system (schematic shown). A computer-controlled switching valve downstream allowed the carrier to pass alternately through a lysine oxidase (LO)-immobilized aminopropyl-glass (APG, pore size 70 nm, 80-120 mesh) enzyme reactor and aa identical reactor containing APG only. The H2O2 (I) produced by the enzyme reactor was detected electrochemically at 10°C. The calibration graph was linear up to the mM range of I and the detection limit was of the order of tens of µM. The RSD (n = 8) was 1.45% for 0.5 mM I. Results agreed well with those obtained by HPLC.
Feed Squid Meal Whitefish Meal Amperometry Electrochemical analysis Sensor Method comparison Immobilized enzyme Buffer Computer Glass beads Valve

"Flow-through Enzyme Analyser For Determination Of L-lysine Concentration"
Biosens. Bioelectron. 1991 Volume 6, Issue 2 Pages 93-99
A. L. Simonian, G. E. Khachatrian, S. Sh. Tatikian, Ts. M. Avakian and I. E. Badalian

Abstract: The flow-through analyzer was based on an oxygen electrode and L-lysine-2-monooxygenase immobilized on silica gel. A schematic diagram is given of the analyzer. and a cross-section of the measurement cell shows a special construction allowing the buffer and its waste to be placed proportionally under the O electrode. The buffer solution was pumped through a pulse damper into the column containing immobilized enzyme. The sample was dosed by a device which injected 70 µL of sample into the column without interruption of the buffer flow. Oxygen concentration. was measured by means of a Clark membrane electrode (0.5 M KCl solution as the electrolyte, Pt cathode and Ag anode, pulse height -0.65 V). Calibration graphs were rectilinear from 5.5 to 55 mM (1 to 10 g l-1) of L-lysine I at pH 8.2. The analyzer. showed high specificity for I. The response time was 15-30 s, with a total analysis time about 3 min. The immobilized enzyme retained at least 50% of its activity for 2 months. Measurement have been made in the fermentation broth of fermenters and in fodder L-lysine concentrate. The analyzer. can be used autonomously and also with a microcomputer or microprocessor.
Fermentation broth Electrode Buffer Column Computer Immobilized enzyme Silica gel

"A Lysine Dehydrogenase-based Electrode For Biosensing Of L-lysine"
Biosens. Bioelectron. 1992 Volume 7, Issue 5 Pages 323-327
Eithne Dempsey, Joseph Wang*, Ulla Wollenberger and Mehmet Ozsoz, Malcolm R. Smyth

Abstract: An amperometric biosensor for L-lysine based on the recently isolated enzyme lysine dehydrogenase is described. Immobilization of the enzyme onto a platinum electrode is achieved via entrapment within a gelatin support on a cellulose membrane. Anodic detection (at 0.4 V vs. Ag/AgCl) is facilitated by the presence of a redox-mediating ferricyanide ion. The effect of experimental variables such as pH, enzyme loading, applied potential, cofactor and mediator concentrations were evaluated in order to optimize the analytical performance. A detection limit of 7 x 10^-8 M, and linearity up to 7 x 10^-4 M are reported. The fast response permits adaptation for flow injection operation with good precision (RSD = 1.9%) and high sample throughout (40 samples per hour). The high specificity offered by this new enzyme is indicated by the lack of interference by other L-amino acids, alcohols or carbohydrates.
Sensor Amperometry Electrode Electrode Optimization Interferences

"Enzyme Electrode For Specific Determination Of L-lysine"
Biotechnol. Bioeng. 1983 Volume 25, Issue 11 Pages 2557-2566
J. L. Romette, J. S. Yang, H. Kusakabe, D. Thomas

Abstract: L-Lysine α-oxidase from Trichoderma viride Y244-2 was immobilized in gelatin and fixed on a pO sensor. The resulting electrode was used for continuous-flow measurement of L-lysine in a fermenter. Dependence of the signal on the O content of the sample was minimized by the enzyme support properties. The measuring range was 0.2 to 4 mM lysine, and the membrane showed good stability over 6 months or for 3000 measurements. Selectivity with respect to other amino-acids was evaluated.
Fermentation broth Electrode Immobilized enzyme