Description
Candida antarctica lipase B (CALB) is widely used in biocatalysis with applications in plasticsdegradation and chemical synthesis. CALB is activated by hydrophobic matrices and shows
striking activation in polar, choline-based, Deep Eutectic Solvents (DES). CALB activation and
stabilisation by tetraalkylammonium (TAA) is caused by binding to choline’s TAA moiety.
Several related TAA salts also caused CALB activation which was proportional to the
hydrophobicity of their alkyl substituents. Notably, tetraoctylammonium bromide showed
activation of ~500% even at low micromolar levels. These TAA salts represent a new class of
enzyme activator. Molecular modelling identified the possible alkylammonium binding location
as a hydrophobic patch centred around Asp-145 of CALB and binding at this site could explain
lipase activation in polar DES solvents.
CALB, like many lipases, is activated by calcium. Intriguingly, mixed soluble activator
experiments showed that calcium and choline bind to different CALB sites, suggesting a twosite model for CALB activation. These observations, along with previous findings, show that
TAA activation is a wider property of enzymes and constitutes a novel and potent means to
enhance enzyme turnover and stability
| Period | 17 Apr 2026 |
|---|---|
| Event title | Cozyme COST action working group meeting |
| Event type | Conference |
| Location | Belgrade, SerbiaShow on map |