645-14-7Relevant articles and documents
Redox hydrogel-based amperometric bienzyme electrodes for fish freshness monitoring
Niculescu, Mihaela,Nistor, Catalin,Frebott, Ivo,Pec, Pavel,Mattiasson, Bo,Csoeregi, Elisabeth
, p. 1591 - 1597 (2000)
This work presents the design and optimization of amperometric biosensors for the determination of biogenic amines (e.g., histamine, putrescine, cadaverine, tyramine, cystamine, agmatine, spermidine), commonly present in food products, and their application for monitoring of freshness in fish samples. The biosensors were used as the working electrodes of a three-electrode electrochemical cell of wall-jet type, operated at -50 mV vs Ag/AgCl, in a flow injection system. Two different bienzyme electrode designs were considered, one based on the two enzymes [a newly isolated and purified amine oxidase (AO) and horseradish peroxidase (HRP)] simply adsorbed onto graphite electrodes, and one when they were cross-linked to an Os-based redox polymer. The redox hydrogel-based biosensors showed better biosensors characteristics, i.e., sensitivity of 0.194 A M-1 cm-2 for putrescine and 0.073 A M-1 cm-2 for histamine, and detection limits (calculated as three times the signal-to-noise ratio) of 0.17 μM for putrescine and 0.33 μM for histamine. The optimized redox hydrogel-based biosensors were evaluated in terms of stability and selectivity, and were used for the determination of total amine content in fish samples kept for 10 days in different conditions.
Magnetic nanoparticles loaded on mobile crystalline material-41: Preparation, characterization and application as a novel material for the construction of an electrochemical nanosensor
Hasanzadeh, Mohammad,Bahrami, Arash,Alizadeh, Mohammad,Shadjou, Nasrin
, p. 24237 - 24246 (2013)
Herein, we envisage the possibility of preparing stable magnetic mobile crystalline material-41 using cetyltrimethylammonium bromide and Fe 3O4 nanoparticles. The Fe3O4 nanoparticles are incorporated into mobile crystalline material-41 in hydrothermal conditions. The prepared mesoporous sample was characterized by Fourier transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), scanning electron microscopy (SEM) and nitrogen adsorption-desorption techniques. The electrochemical behavior of cadaverine, histamine and putrescine was investigated on magnetic mobile crystalline material-41 (MCM-41-Fe 2O3) modified carbon paste electrodes (CPEs). Due to the very large surface area (1213 m2 g-1) and the remarkable electrocatalytic properties of Fe2O3 nanoparticles, MCM-41-Fe2O3 exhibits potent electrocatalytic activity toward the electrooxidation of some selected biogenic amines. MCM-41-Fe 2O3-CPEs provide new capabilities for electrochemical sensing by combining the advantages of Fe2O3 magnetic nanoparticles and MCM-41 with a very large surface area. The process of oxidation and its kinetics were established by using cyclic voltammetry, chronoamperometry techniques, and also, steady state polarization measurements. The apparent electron transfer rate constant (Ks) and transfer coefficient (α) were determined by cyclic voltammetry and were approximately 6.2 s-1 and 0.48, respectively. The linear concentration ranges of the proposed sensors for cadaverine, histamine and putrescine were 0.1-10, 0.01-0.5 and 0.9-35 μM, respectively. Finally, the applicability of the sensor to the determination of electroactive biogenic amine concentrations in fish samples has been successfully demonstrated.
The isolation of iminazole acetaldehyde as the only metabolite of the action in vitro of placental histaminase on histamine.
KAPELLER-ADLER
, p. 527 - 530 (1960)
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Influence of copper(II) catalyst on the oxidation of l-histidine by platinum(IV) in alkaline medium: A kinetic and mechanistic study
Fawzy, Ahmed
, p. 567 - 576 (2014)
The kinetics of oxidation of l-histidine (His) by platinum(IV) in the absence and presence of copper(II) catalyst was studied using spectrophotometry in alkaline medium at a constant ionic strength of 0.1 mol dm-3 and at 25°C. In both cases, the reactions exhibit a 1:1 stoichiometry ([His]:[PtIV]). The rate of the uncatalyzed reaction is dependent on the first power of each of the concentrations of oxidant, substrate and alkali. The catalyzed path shows a first-order dependence on both [PtIV] and [CuII], but the order with respect to both [His] and [OH-] is less than unity. The rate constants increase with increasing ionic strength and dielectric constant of the medium. The catalyzed reaction has been shown to proceed via formation of a copper(II)-histidine intermediate complex, which reacts with the oxidant by an inner-sphere mechanism leading to decomposition of the complex in the rate-determining step. Platinum(IV) is reduced to platinum(II) by the substrate in a one-step two-electron transfer process. This is followed by other fast steps, giving rise to the oxidation products which were identified as 2-imidazole acetaldehyde, ammonia and carbon dioxide. A tentative reaction mechanism is suggested, and the associated rate laws are deduced. The activation parameters with respect to the slow step of the mechanism are reported and discussed.
A single amino acid substitution converts a histidine decarboxylase to an imidazole acetaldehyde synthase
Takeshima, Daiki,Mori, Ayaka,Ito, Hideyuki,Komori, Hirofumi,Ueno, Hiroshi,Nitta, Yoko
, (2020/09/09)
Histidine decarboxylase (HDC; EC 4.1.1.22), an enzyme that catalyzes histamine synthesis with high substrate specificity, is a member of the group II pyridoxal 5′-phosphate (PLP) -dependent decarboxylase family. Tyrosine is a conserved residue among group II PLP-dependent decarboxylases. Human HDC has a Y334 located on a catalytically important loop at the active site. In this study, we demonstrated that a HDC Y334F mutant is capable of catalyzing the decarboxylation-dependent oxidative deamination of histidine to yield imidazole acetaldehyde. Replacement of the active-site Tyr with Phe in group II PLP-dependent decarboxylases, including mammalian aromatic amino acid decarboxylase, plant tyrosine/DOPA decarboxylase, and plant tryptophan decarboxylase, is expected to result in the same functional change, given that a Y-to-F substitution at the corresponding residue (number 260) in the HDC of Morganella morganii, another group II PLP-dependent decarboxylase, yielded the same effect. Thus, it was suggested that the loss of the OH moiety from the active-site Tyr residue of decarboxylase uniquely converts the enzyme to an aldehyde synthase.
