TY - JOUR
T1 - Optimised Protocol for Drying Aqueous Enzyme Solutions in Organic Solvents – Comparison of Free and Immobilised Candida antarctica Lipase B
AU - Tjørnelund, Helena D.
AU - Brask, Jesper
AU - Woodley, John M.
AU - Peters, Günther H.J.
PY - 2023
Y1 - 2023
N2 - Here, we propose an optimised protocol for controlling the initial water
activity (aw) in organic reaction mixtures with soluble lipase to
ensure reproducible and consistent enzyme activity measurements.
Pre-equilibration above saturated salt solutions was used to set aw of
the reaction media, where aw was tracked with a hygrometer. Consistent
stirring of the suspension and volume correction to compensate for
solvent evaporation were found to be critical. The protocol was tested
on Candida antarctica lipase B (CALB) in soluble and immobilised forms
in three organic solvents (acetonitrile, methyl tert-butyl ether, and
hexane) at four different water activities ranging from 0.12 to 0.97.
Soluble and immobilised CALB had similar aw-profiles and showed the
highest enzyme activity in hexane. The optimised protocol expands the
possibility to study enzyme kinetics from immobilised enzymes to soluble
enzymes.
AB - Here, we propose an optimised protocol for controlling the initial water
activity (aw) in organic reaction mixtures with soluble lipase to
ensure reproducible and consistent enzyme activity measurements.
Pre-equilibration above saturated salt solutions was used to set aw of
the reaction media, where aw was tracked with a hygrometer. Consistent
stirring of the suspension and volume correction to compensate for
solvent evaporation were found to be critical. The protocol was tested
on Candida antarctica lipase B (CALB) in soluble and immobilised forms
in three organic solvents (acetonitrile, methyl tert-butyl ether, and
hexane) at four different water activities ranging from 0.12 to 0.97.
Soluble and immobilised CALB had similar aw-profiles and showed the
highest enzyme activity in hexane. The optimised protocol expands the
possibility to study enzyme kinetics from immobilised enzymes to soluble
enzymes.
U2 - 10.1002/cctc.202201207
DO - 10.1002/cctc.202201207
M3 - Journal article
SN - 1867-3880
VL - 15
JO - ChemCatChem
JF - ChemCatChem
IS - 1
M1 - e202201207
ER -