Article Dans Une Revue ChemBioChem Année : 2024

Ether Bond Cleavage of a Phenylcoumaran β‐5 Lignin Model Compound and Polymeric Lignin Catalysed by a LigE‐type Etherase from Agrobacterium sp.

Résumé

A LigE-type beta-etherase enzyme from lignin-degrading Agrobacterium sp. has been identified, which assists degradation of polymeric lignins. Testing against lignin dimer model compounds revealed that it does not catalyse the previously reported reaction of Sphingobium SYK-6 LigE, but instead shows activity for a β-5 phenylcoumaran lignin dimer. The reaction products did not contain glutathione, indicating a catalytic role for reduced glutathione in this enzyme. Three reaction products were identified: the major product was a cis-stilbene arising from CÀ C fragmentation involving loss of formaldehyde; two minor products were an alkene arising from elimination of glutathione, and an oxidised ketone, proposed to arise from reaction of an intermediate with molecular oxygen. Testing of the recombinant enzyme against a soda lignin revealed the formation of new signals by two-dimensional NMR analysis, whose chemical shifts are consistent with the formation of a stilbene unit in polymeric lignin.

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hal-05188494 , version 1 (10-10-2025)

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Goran M M Rashid, Guillaume N Rivière, Betty Cottyn‐boitte, Amel Majira, Laurent Cézard, et al.. Ether Bond Cleavage of a Phenylcoumaran β‐5 Lignin Model Compound and Polymeric Lignin Catalysed by a LigE‐type Etherase from Agrobacterium sp.. ChemBioChem, 2024, 25 (8), pp.e202400132. ⟨10.1002/cbic.202400132⟩. ⟨hal-05188494⟩
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