References of "Granier, Benoît"
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See detailPreliminary Evaluation of Antimicrobial Residue Levels in Marketed Pork and Chicken Meat in the Red River Delta Region of Vietnam
pham kim, Dang; Degand, Guy ULg; Douny, Caroline ULg et al

in Food and Public Health (2013), 3(6), 267-276

The presence of antibacterial in 97 pork and 83 chicken meat samples, randomly collected from 3 different representative provinces (Hanoi, Hai Duong and Thai Binh) of the Red River Delta, was determined ... [more ▼]

The presence of antibacterial in 97 pork and 83 chicken meat samples, randomly collected from 3 different representative provinces (Hanoi, Hai Duong and Thai Binh) of the Red River Delta, was determined by a screening step using in parallel 2 microbiological methods (Premi®-test and New Two Plate Test). In total, 27% of all samples displayed a positive response in at least one of both tests, from which 11 (13% of chicken samples) are chicken samples and 38 (39% of pork samples) are pork samples. The 33 samples from the Thai Binh which were screened positive were then submitted to post-screening tests specific for tetracyclines and (fluoro) quinolones (Tetrasensor® dipstick for tetracyclines and an ELISA for quinolones), two groups of antibiotics widely used in animal production in this region, and confirmed by liquid chromatography coupled to mass spectrometry. Tetracyclines and (fluoro)quinolones residues were found, using a post screening test, in 23 and 5 samples, respectively. Ten (all pork) and 4 samples (1 pork, 3 chicken) were confirmed containing tetracyclines (chlortetracycline, oxytetracycline, tetracycline, doxycycline) and (fluoro) quinolones (nalidixic acid, enrofloxacin and ciprofloxacin) respectively, from which 1 and 3 pork samples were found to contain enrofloxacin and tetracycline residues , respectively, with a concentration higher than their respective MRLs. This study shows the good performance of the proposed strategy to identify non-compliant meat samples (microbiological screening, tetracyclines and quinolones targeted post-screening and confirmation), which allows to obtain conclusive results in 82% of the cases. [less ▲]

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See detailScreening, post-screening and confirmation analysis of antibiotics in pork and chicken meat marketed in Vietnam.
Pham Kim, Dang; Degand, Guy ULg; Douny, Caroline ULg et al

in EuroResidue VII: conference on residues of veterinary drugs in food (2012)

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See detailSolubilisation and binding characteristics of a recombinant beta(2)-adrenergic receptor expressed in the membrane of Escherichia coli for the multianalyte detection of beta-agonists and antagonists residues in food-producing animals
Danyi, Sophie ULg; Degand, Guy ULg; Duez, Colette ULg et al

in Analytica Chimica Acta (2007), 589(2), 159-165

The number of substances with beta-agonistic activity, illegally introduced in meat production or in sports doping as anabolic or beta-blocking agents is increasing. Analytical methods suited for their ... [more ▼]

The number of substances with beta-agonistic activity, illegally introduced in meat production or in sports doping as anabolic or beta-blocking agents is increasing. Analytical methods suited for their multianalyte detection are thus necessary. In this perspective, receptor assays were developed. The research activities undertaken in this study describe the solubilisation of a recombinant human beta(2)-adrenergic receptor produced in the inner membrane of genetically modified Escherichia coli, using the detergent n-dodecyl-beta-D-maltoside. Its potential to detect the presence of beta-agonists or beta-blockers in biological samples was evaluated. The solubilised beta(2)-adrenergic receptor retained its binding affinity in a radio-receptor assay based on the competition for the binding to receptors between a ligand (beta-agonist or antagonist) and the radioligand [I-125]iodocyanopindolol. The IC50 values ranged from 5 +/- x 10(-8) M (clenbuterol) to 8 +/- 2 x 10(-6) M (isoxsuprine) for the beta-agonists tested and from 1.5 +/- 0.2 x 10(-10) M (carazolol) to 1.2 +/- 0.2 x 10(-5) M (metoprolol) for the beta-blockers tested. It was shown to have a lower limit of detection than a radio-receptor assay using the solubilised beta(2)-adrenoceptor expressed in a mammalian cell line. The solubilised recombinant human beta(2)-adrenoreceptor expressed in E. coli would be a useful tool to develop non radioactive multianalyte screening methods. (c) 2007 Elsevier B.V. All rights reserved. [less ▲]

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See detailThe kinetic properties of the carboxy terminal domain of the Bacillus licheniformis 749/I BlaR penicillin-receptor shed a new light on the derepression of beta-lactamase synthesis
Duval, Valérie; Swinnen, Marc; Lepage, Sophie et al

in Molecular Microbiology (2003), 48(6), 1553-1564

To study the properties of the BlaR penicillin-receptor involved in the induction of the Bacillus licheniformis beta-lactamase, the water-soluble carboxy terminal domain of the protein (BlaR-CTD) was ... [more ▼]

To study the properties of the BlaR penicillin-receptor involved in the induction of the Bacillus licheniformis beta-lactamase, the water-soluble carboxy terminal domain of the protein (BlaR-CTD) was overproduced in the periplasm of Escherichia coli JM105 and purified to protein homogeneity. Its interactions with various beta-lactam antibiotics were studied. The second-order acylation rate constants k(2)/K' ranged from 0.0017 to more than 1 muM(-1) s(-1) and the deacylation rate constants were lower than 4x10(-5) s(-1) . These values imply a rapid to very rapid formation of a stable acylated adduct. BlaR-CTD is thus one of the most sensitive penicillin-binding proteins presently described. In the light of these results, the kinetics of beta-lactamase induction in Bacillus licheniformis were re-examined. When starting with a rather high cell density, a good beta-lactamase substrate such as benzylpenicillin is too sensitive to beta-lactamase-mediated hydrolysis to allow full induction. By contrast, a poor beta-lactamase substrate (7-aminocephalosporanic acid) can fully derepress beta-lactamase expression under conditions where interference of the antibiotic with cell growth is observed. These results suggest that acylation of the penicillin receptor is a necessary, but not sufficient, condition for full induction. [less ▲]

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See detailThe Precursor of the Streptomyces R61 Dd-Peptidase Containing a C-Terminal Extension Is Inactive
Fanuel, Laurence; Granier, Benoît; Wilkin, Jean-Marc et al

in FEBS Letters (1994), 351(1), 49-52

The Streptomyces R61 DD-peptidase gene encodes a 26-residue C-terminal extension which is not found in the mature protein. When the gene was expressed in Escherichia coli, the extension was not cleaved ... [more ▼]

The Streptomyces R61 DD-peptidase gene encodes a 26-residue C-terminal extension which is not found in the mature protein. When the gene was expressed in Escherichia coli, the extension was not cleaved and the precursor protein was not enzymatically active. It also reacted with penicillins significantly more slowly than the mature protein. The introduction of a 'stop' codon after that corresponding to the C-terminal residue of the mature protein resulted in the production of an active protein in the periplasm of E. coli. [less ▲]

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See detailSerine-Type D-Ala-D-Ala Peptidases and Penicillin-Binding Proteins
Granier, Benoît; Jamin, Marc; Adam, Maggy et al

in Methods in Enzymology (1994), 244

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See detailUse of neural networks for monitoring a bioreactor
Groslambert, Sylvie ULg; Granier, Benoit; Marchot, Pierre ULg et al

Poster (1993)

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See detailPrimary and Predicted Secondary Structures of the Actinomadura R39 Extracellular DD-Peptidase, a Penicillin-Binding Protein (PBP) Related to the Escherichia coli PBP4
Granier, Benoît; Duez, Colette ULg; Englebert, Serge et al

in Biochemical Journal (1992), 282(Pt 3), 781-788

As derived from gene cloning and sequencing, the 489-amino-acid DD-peptidase/penicillin-binding protein (PBP) produced by Actinomadura R39 has a primary structure very similar to that of the Escherichia ... [more ▼]

As derived from gene cloning and sequencing, the 489-amino-acid DD-peptidase/penicillin-binding protein (PBP) produced by Actinomadura R39 has a primary structure very similar to that of the Escherichia coli PBP4 [Mottl, Terpstra & Keck (1991) FEMS Microbiol. Lett. 78, 213-220]. Hydrophobic-cluster analysis of the two proteins shows that, providing that a large 174-amino-acid stretch is excluded from the analysis, the bulk of the two polypeptide chains possesses homologues of the active-site motifs and secondary structures found in the class A β-lactamase of Streptomyces albus G of known three-dimensional structure. The 74-amino-acid insert occurs at equivalent places in the two PBPs, between helices α2 and α3, away from the active site. Such an insert is unique among the penicilloyl serine transferases. It is proposed that the Actinomadura R39 PBP and E. coli PBP4 form a special class, class C, of low-Mr PBPs/DD-peptidases. A vector has been constructed and introduced by electrotransformation in the original Actinomadura R39 strain, allowing high-level expression and secretion of the DD-peptidase/PBP (250 mg . 1-1). The gene encoding the desired protein is processed differently in Actinomadura R39 and Streptomyces lividans. Incorrect processing in Streptomyces lividans leads to a secreted protein which is inert in terms of DD-peptidase activity and penicillin-binding capacity. [less ▲]

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See detailUse of neural networks for monitoring a bioreactor
Groslambert, Sylvie ULg; Granier, Benoit; Marchot, Pierre ULg et al

Poster (1991)

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