Enzyme-Linked Aptamer Assays (Elaas), Based On A Competition Format For A Rapid And Sensitive Detection Of Ochratoxin A In Wine

ISI Document Delivery No.: 715BU Times Cited: 29 Cited Reference Count: 32 Cited References: Alarcon SH, 2006, TALANTA, V69, P1031, DOI 10.1016/j.talanta.2005.12.024 Amezqueta S, 2009, FOOD CONTROL, V20, P326, DOI 10.1016/j.foodcont.2008.05.017 [Anonymous], 2005, OFFICIAL J EUROPEA L, VL25, P3 Baldrich E, 2005, ANAL CHEM, V77, P4774, DOI 10.1021/ac0502450 Brody E. N., 2000, REV MOL BIOTECHNOL, V74, P5, DOI DOI 10.1016/S1389-0352(99)00004-5 Bruno JG, 2009, J FLUORESC, V19, P427, DOI 10.1007/s10895-008-0429-8 Burdaspal P, 2007, FOOD ADDIT CONTAM, V24, P976, DOI 10.1080/02652030701311155 Cruz-Aguado JA, 2008, J AGR FOOD CHEM, V56, P10456, DOI 10.1021/jf801957h Cruz-Aguado JA, 2008, ANAL CHEM, V80, P8853, DOI 10.1021/ac8017058 De Saeger S, 2002, INT J FOOD MICROBIOL, V75, P135, DOI 10.1016/S0168-1605(01)00749-8 ELLINGTON AD, 1990, NATURE, V346, P818, DOI 10.1038/346818a0 Hamula CLA, 2006, TRAC-TREND ANAL CHEM, V25, P681, DOI 10.1016/j.trac.2006.05.007 Jayasena SD, 1999, CLIN CHEM, V45, P1628 JENISON RD, 1994, SCIENCE, V263, P1425, DOI 10.1126/science.7510417 Joshi R, 2009, MOL CELL PROBE, V23, P20, DOI 10.1016/j.mcp.2008.10.006 Mairal T, 2008, ANAL BIOANAL CHEM, V390, P989, DOI 10.1007/s00216-007-1346-4 Mann D, 2005, BIOCHEM BIOPH RES CO, V338, P1928, DOI 10.1016/j.bbrc.2005.10.172 Ngundi MM, 2005, ANAL CHEM, V77, P148, DOI 10.1021/ac048957y Papamichael KI, 2007, SENSOR ACTUAT B-CHEM, V121, P178, DOI 10.1016/j.snb.2006.09.024 Prieto-Simon B, 2008, BIOSENS BIOELECTRON, V23, P995, DOI 10.1016/j.bios.2007.10.002 Radi AE, 2009, ELECTROCHIM ACTA, V54, P2180, DOI 10.1016/j.electacta.2008.10.013 Radoi A, 2009, ANAL LETT, V42, P1187, DOI 10.1080/00032710902890447 Ricci F, 2007, ANAL CHIM ACTA, V605, P111, DOI 10.1016/j.aca.2007.10.046 Rusanova TY, 2009, ANAL CHIM ACTA, V653, P97, DOI 10.1016/j.aca.2009.08.036 Stoltenburg R, 2007, BIOMOL ENG, V24, P381, DOI 10.1016/j.bioeng.2007.06.001 Tombelli S, 2007, BIOMOL ENG, V24, P191, DOI 10.1016/j.bioeng.2007.03.003 TUERK C, 1990, SCIENCE, V249, P505, DOI 10.1126/science.2200121 Turner NW, 2009, ANAL CHIM ACTA, V632, P168, DOI 10.1016/j.aca.2008.11.010 van der Gaag B, 2003, FOOD CONTROL, V14, P251, DOI 10.1016/S0956-7135(03)00008-2 Wilson C, 1998, CHEM BIOL, V5, P609, DOI 10.1016/S1074-5521(98)90289-7 Wochner A, 2007, BIOTECHNIQUES, V43, P344, DOI 10.2144/000112532 Zezza F, 2009, ANAL BIOANAL CHEM, V395, P1317, DOI 10.1007/s00216-009-2994-3 Barthelmebs, Lise Jonca, Justyna Hayat, Akhtar Prieto-Simon, Beatriz Marty, Jean-Louis Higher Education Commission of Pakistan Akhtar HAYAT benefits from a grant of Higher Education Commission of Pakistan. The authors are very grateful to Richard Cooke and Michele Laudie from the LGDP of Perpignan University for aptamer sequencing and to Soft Flow Biotechnology for kindly providing the monoclonal antibody. 30 ELSEVIER SCI LTD OXFORD FOOD CONTROLOchratoxin A (OTA) is one of the most important mycotoxins because of its high toxicity to both humans and animals and its occurrence in a number of basic foods and agro-products. The need to develop high-performing methods for OTA analysis able to improve the traditional ones is evident. In this work, through in vitro SELEX (Systematic Evolution of Ligands by EXponential enrichment) two aptamers, designated H8 and H12 were produced that bind with nanomolar affinity with Ochratoxin A (OTA). Two strategies were investigated by using an indirect and a direct competitive Enzyme-Linked Aptamer Assay (ELAA) and were compared to the classical competitive Enzyme-Linked Immunosorbent Assay (ELISA) for the determination of OTA in spiked red wine samples. The limit of detection attained (1 ng/mL), the midpoint value obtained (5 ng/mL) and the analysis time needed (125 min) for the real sample analysis validate the direct competitive ELAA as useful screening tool for routine use in the control of OTA level in wine. (C) 2010 Elsevier Ltd. All rights reserved

Organometallic synthesis of CuO nanoparticles: Application in low-temperature CO detection

International audienceA metal–organic approach has been employed for the preparation of anisotropic CuO nanoparticles. These nanostructures have been characterized by transmission and high resolution transmission electron microscopy, field‐emission scanning electron microscopy, X‐ray powder diffraction, Fourier transform infrared spectroscopy and X‐ray photoelectron spectroscopy. The CuO nanoparticles have been deposited as gas‐sensitive layers on miniaturized silicon devices. At an operating temperature of 210 °C, the sensors present an optimum response toward carbon monoxide correlated with a fast response (Rn) and short recovery time. A high sensitivity to CO (Rn≈150 %, 100 ppm CO, RH 50 %) is achieved. These CuO nanoparticles serve as a very promising sensing layer for the fabrication of selective CO gas sensors working at a low temperature

Pectobacterium zantedeschiae sp. nov. a new species of a soft rot pathogen isolated from Calla lily (Zantedeschia spp.)

Four Gram-negative, rod-shaped pectinolytic bacterial strains designated as 2M, 9M, DPMP599 and DPMP600 were subjected to polyphasic analyses that revealed their distinctiveness from the other Pectobacterium species. Strains 2M and 9M were isolated from Calla lily bulbs cultivated in Central Poland. DPMP599 and DPMP600 strains were isolated from Calla lily leaves from plants grown in Serbia. Phylogenetic analyses based on nine housekeeping genes (gapA, gyrA, icdA, pgi, proA, recA, recN, rpoA, and rpoS), as well as phylogeny based on the 381 most conserved universal proteins confirmed that Pectobacterium zantedeschiae strains were distantly related to the other Pectobacterium, and indicated Pectobacterium atrosepticum, Pectobacterium betavasculorum, Pectobacterium parmentieri and Pectobacterium wasabiae as the closest relatives. Moreover, the analysis revealed that Pectobacterium zantedeschiae strains are not akin to Pectobacterium aroidearum strains, which were likewise isolated from Calla lily. The genome sequencing of the strains 2M, 9M and DPMP600 and their comparison with whole genome sequences of other Pectobacterium type strains confirmed their distinctiveness and separate species status within the genus based on parameters of in silico DNA–DNA hybridization and average nucleotide identity (ANI) values. The MALDI-TOF MS proteomic profile supported the proposition of delineation of the P. zantedeschiae and additionally confirmed the individuality of the studied strains. Based on of all of these data, it is proposed that the strains 2M, 9M, DPMP599, and DPMP600 isolated from Calla lily, previously assigned as P. atrosepticum should be reclassified as Pectobacterium zantedeschiae sp. nov. with the strain 9M T (PCM2893 = DSM105717 = IFB9009) as the type strain