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;...
Published in: | Journal of Molecular Catalysis B: Enzymatic |
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Main Authors: | , , , , , , |
Format: | Text |
Language: | English |
Published: |
2021
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Subjects: | |
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 |
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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