Size selectivity in lipase catalysed tetrol acylation

Size selectivity of Candida antarctica lipase B (CAL-B) was examined in the acylation of pentaerythritol with oleic acid. Biolubricant mixtures consisting of mono-, di-, tri-, and tetraoleates were expected in variable excess. Enzymatic tetraoleate formation was suppressed under solvent conditions;...

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Bibliographic Details
Published in:Journal of Molecular Catalysis B: Enzymatic
Main Authors: Happe, Manuel, Kouadio, Martial, Treanor, Christopher, Sawal, Jan-Phillip, Fornage, Antoine, Sugnaux, Marc, Fischer, Fabian
Format: Text
Language:English
Published: 2021
Subjects:
Antarc*
Antarctica
Online Access:https://doi.org/10.1016/j.molcatb.2014.08.004
https://arodes.hes-so.ch/record/8843/files/Published%20version.pdf
http://arodes.hes-so.ch/record/8843
Description
Summary:Size selectivity of Candida antarctica lipase B (CAL-B) was examined in the acylation of pentaerythritol with oleic acid. Biolubricant mixtures consisting of mono-, di-, tri-, and tetraoleates were expected in variable excess. Enzymatic tetraoleate formation was suppressed under solvent conditions; however, this size selectivity was lost without solvent and tetra-acylated pentaerythritol accumulated in up to 93%. The lipase caused size selectivity persisted over a broad temperature range from 35 to 95 °C. A Fischer–Speier esterification showed that substrate bulkiness was only a minor contributor to observed size selectivity. All in all, switch on/off size selectivity using CAL-B allowed to vary pentaerythritol biolubricant compositions in an unprecedented manner.

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