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Design of chromogenic probes for efficient screening and evaluation of feruloyl esterase-like activities

Olga Gherbovet 1 Régis Fauré 1 Fernando Ferreira 1 Julien Durand 1 Mélanie Ragon 1 Guillaume Hostyn 1 Eric Record 2 Sophie Bozonnet 1 Michael O'Donohue 1
1 LISBP - Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés
2 BBF - Biodiversité et Biotechnologie Fongiques
Abstract : Feruloyl esterases (FAEs) constitute an important sub-group of hydrolytic enzymes involved in the deconstruction of plant cell wall polysaccharides. However, in the current era of genomics and metagenomics, finding and characterizing FAEs is not straightforward, mainly due to a lack of suitable compounds for high-throughput assays. To remedy this, indolyl and 4-nitrocatechol hydroxycinnamates (i.e. transferulate and p-coumarate derivatives) were synthesized in good overall yields-between 46 and 56% after 4 steps- and their usefulness as substrates for FAEs was ascertained. The hydrolysis of the ester bond of these chromogenic compounds leads to a colour change, which can be readily monitored. Overall, these compounds considerably improve upon the current situation and enable the measurement of FAE activities in both qualitative solid medium-based and quantitative liquid assays.
Keywords : ASPERGILLUS-NIGER SPECTROPHOTOMETRIC ASSAY DIRECTED EVOLUTION BIOMASS DIFFERENTIATION SPECIFICITY CLASSIFICATION SUBSTRATE ENZYME BIOCATALYSTS
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Journal articles
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https://hal-amu.archives-ouvertes.fr/hal-01450768
Contributor : Sabine Genet <>
Submitted on : Tuesday, January 31, 2017 - 1:15:36 PM
Last modification on : Monday, October 26, 2020 - 3:47:07 PM

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UNIV-AMU | CNRS | INRA | EC-MARSEILLE | INSA-TOULOUSE | INSA-GROUPE | AGROSUP-DIJON | AGROSUP-PAM | TBI | INRAE

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Olga Gherbovet, Régis Fauré, Fernando Ferreira, Julien Durand, Mélanie Ragon, et al.. Design of chromogenic probes for efficient screening and evaluation of feruloyl esterase-like activities. Journal of Molecular Catalysis B: Enzymatic, Elsevier, 2016, 126, pp.24-31. ⟨10.1016/j.molcatb.2016.01.012⟩. ⟨hal-01450768⟩

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