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Diesterification of 3‐[(β‐Cyclodextrinyl)succinamido]propane‐1,2‐diol Catalysed by Lipase: Diastereoselectivity or Tridimensional Substrate Specificity?
Author(s) -
Gervaise Cédric,
Bonnet Véronique,
Nolay Florian,
Cézard Christine,
Stasik Imane,
Sarazin Catherine,
DjedaïniPilard Florence
Publication year - 2014
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.201402414
Subject(s) - diastereomer , lipase , chemistry , substrate (aquarium) , selectivity , transesterification , diol , organic chemistry , stereochemistry , catalysis , enzyme , biology , ecology
The transesterification of 3‐[(β‐cyclodextrinyl)succinamido]propane‐1,2‐diol with fatty esters catalyzed by immobilized lipase from Mucor miehei occurred with very different conversions of the two diastereoisomers [( R )‐ or ( S )‐amidopropanediol]. The highest conversion observed with the ( S )‐amidopropanediol can be related to either lipase diastereoselectivity or substrate specificity. To investigate the diastereoselectivity of the lipase, diastereoisomers of the methylated β‐cyclodextrin were replaced by methylated glucopyranoside or methylleucine. No discrimation of the diastereoisomers by lipase was observed. Molecular modeling was performed to assess the lipase selectivity towards the two diastereoisomers. It was found that the ( R )‐amidopropanediol is stabilized by hydrogen bonding with the cyclodextrin rim resulting in less reactive hydroxy groups.