Laurence Fanuel

Laurence Fanuel
Art Gallery in historical Grasse Center

Ph.D. Biochemistry - Senior Perfumer

About

14
Publications
936
Reads
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451
Citations
Citations since 2016
2 Research Items
83 Citations
2016201720182019202020212022051015
2016201720182019202020212022051015
2016201720182019202020212022051015
2016201720182019202020212022051015
Introduction
From biochemistry study to human emotion study: linking physiology and psychology through artistic creation and emotion self-awareness became important to work on global better life quality
Additional affiliations
September 1994 - September 1999
University of Liège
Position
  • Ph.D student FNRS

Publications

Publications (14)
Article
Odors are deep triggers of emotions. As per research by Thomas Hummel (1) with people who have lost the sense of smell, odors seem to be at the crossroad of the other senses, making the full picture more complete and to be immersed in it. Based on these observations, we - Christine Glen, painter, and Laurence Fanuel, perfumer, with Olivier Wahl, ar...
Chapter
Une pièce de théâtre odorisée suppose la collaboration entre metteur en scène et parfumeur pour créer les odeurs adéquates et les intégrer au jeu des acteurs. Laurence Fanuel analyse l'expérience de parfumeur hors-piste qui l'a conduite à odoriser Les Parfums de l'Ame et le mouvement de synergie entre son art et celui de l'auteure et menteuse en sc...
Conference Paper
Full-text available
Laurence Fanuel, a perfumer and senior scientist with Takasago International, is a passionate advocate of the art of fragrance, its role in our lives and the benefits it can bring. Originally from Belgium, Laurence now lives and works in Paris. She was educated at Liege University in Belgium where she attained her Ph.D in biochemistry. She joined P...
Article
Different strains of Bacillus were screened for their ability to hydrolyse D-alanyl-p-nitroanilide. Activity was detected in Bacillus pumilus, Bacillus brevis, Bacillus licheniformis 749I and Bacillus subtilis 168. The last strain was the best producer and was selected for the production and purification of the enzyme. The determination of the N-te...
Article
Different strains of Bacillus were screened for their ability to hydrolyse d-alanyl-p-nitroanilide. Activity was detected in Bacillus pumilus, Bacillus brevis, Bacillus licheniformis 749I and Bacillus subtilis 168. The last strain was the best producer and was selected for the production and purification of the enzyme. The determination of the N-te...
Article
Full-text available
beta-Lactam compounds are the most widely used antibiotics. They inactivate bacterial DD-transpeptidases, also called penicillin-binding proteins (PBPs), involved in cell-wall biosynthesis. The most common bacterial resistance mechanism against beta-lactam compounds is the synthesis of beta-lactamases that hydrolyse beta-lactam rings. These enzymes...
Article
Full-text available
The L-aminopeptidase D-Ala-esterase/amidase from Ochrobactrum anthropi (DmpA) releases the N-terminal L and/or D-Ala residues from peptide substrates. This is the only known enzyme to liberate N-terminal amino acids with both D and L stereospecificity. The DmpA active form is an alphabeta heterodimer, which results from a putative autocatalytic cle...
Article
Full-text available
The DmpA (d-aminopeptidase A) protein produced by Ochrobactrum anthropi hydrolyses p-nitroanilide derivatives of glycine and d-alanine more efficiently than that of l-alanine. When regular peptides are utilized as substrates, the enzyme behaves as an aminopeptidase with a preference for N-terminal residues in an l configuration, thus exemplifying a...
Article
Full-text available
Two new enzymes which hydrolyse D-alanyl-p-nitroanilide have been detected in Ochrobactrum anthropi LMG7991 extracts. The first enzyme, DmpB, was purified to homogeneity and found to be homologous to the Dap protein produced by O. anthropi SCRC C1-38 (ATCC49237). The second enzyme, DmpA, exhibits a similar substrate profile when tested on p-nitroan...
Article
Full-text available
Ochrobactrum anthropi possesses an L-aminopeptidase (DmpA) also able to act as a D-amidase/D-esterase. DmpA (40 kDa) is activated by auto-catalyzed protein splicing liberating an alpha-amino group presumably used as a general base in the catalytic mechanism. Two crystal forms were obtained at 294 K in 13-16% PEG 2000 mono-methylether at pH 9.0, add...
Article
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 intr...
Article
Full-text available
The catalytic properties of three class B beta-lactamases (from Pseudomonas maltophilia, Aeromonas hydrophila and Bacillus cereus) were studied and compared with those of the Bacteroides fragilis enzyme. The A. hydrophila beta-lactamase exhibited a unique specificity profile and could be considered as a rather specific 'carbapenemase'. No relations...

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Projects

Project (1)
Project
well-being, consciousness