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  • Title: The use of enzyme-coupled magnetic nanoparticles for studying the spectra of unusual substrates of mushroom tyrosinase by direct surface-assisted laser desorption/ionisation and high-resolution electrospray ionisation quadrupole-quadrupole-time-of-flight mass spectrometry.
    Author: Salwiński A, Da Silva D, Delépée R, Maunit B.
    Journal: Rapid Commun Mass Spectrom; 2014 Sep 30; 28(18):1957-63. PubMed ID: 25132295.
    Abstract:
    RATIONALE: Tyrosinase-coupled magnetic particles (EMPs) were used to demonstrate that resorcinol-containing tyrosinase inhibitors are oxidised by tyrosinase only in the presence of the enzyme's classic substrate. This shows the potential for the application of EMPs as a non-organic matrix for monitoring enzymatic conversion of a novel substrate family directly on-the-spot, principally due to minimal enzyme requirement per analysis. METHODS: Tyrosinase was covalently coupled to core-shell-type silica-coated iron oxide magnetic nanoparticles (EMPs) that were applied as non-organic SALDI matrix suitable for studying low-mass compounds using a classic matrix-assisted laser desorption/ionisation time-of-flight (MALDI-TOF) mass spectrometer. Because of the dual function of the EMPs - enzyme host and non-organic matrix - we describe this ionisation method as Enzyme-coupled Nanoparticles-Assisted LDI-MS (ENALDI-MS). Supplementary studies of the enzymatic conversion of glabridin and 3-(2,4-dihydroxyphenyl)propionic acid (DHPA) were conducted by high-resolution electrospray ionisation quadrupole-quadrupole-time-of-flight mass spectrometry (ESI-QqTOF-MS). RESULTS: The initial experiment involving EMPs as non-organic matrix (ENALDI-MS) showed enzymatic conversion of glabridin, a strong tyrosinase inhibitor, only in the presence of L-Tyr, the classic tyrosinase substrate. These findings were evaluated by ESI-QqTOF-MS proving that glabridin and DHPA are converted into the corresponding quinones by tyrosinase only in the presence of the auxiliary monophenol or o-diphenol substrates (L-Tyr and catechin, respectively) capable of regenerating the active site of tyrosinase. CONCLUSIONS: EMPs were shown to be useful as a non-organic matrix to monitor enzymatic conversion of the novel tyrosinase substrate family directly on-the-spot with a minimal enzyme consumption (6.5 pmol/spot). Results obtained by ENALDI-MS were fully confirmed by ESI-QqTOF-MS demonstrating that resorcinol-containing tyrosinase inhibitors may be oxidised by the enzyme in the presence of its classic substrates.
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