Size selectivity in lipase catalysed tetrol acylation

作者：Happe Manuel; Kouadio Martial; Treanor Christopher; Sawall Jan Phillip; Fornage Antoine; Sugnaux Marc; Fischer Fabian^*

来源：Journal of Molecular Catalysis B: Enzymatic , 2014, 109: 40-46.

DOI：10.1016/j.molcatb.2014.08.004

• Lipase
• Biolubricant
• Esterification
• Size-selectivity
• Solvent effect

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 degrees 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.

• 出版日期2014-11