Immobilization of lipases has proved to be a useful technique for improving an enzyme's activity in organic solvents.
METHODS AND RESULTS:
In the present study, the performance of a silica-immobilized lipase was evaluated for the synthesis of Isopropyl ferulate in DMSO. The biocatalyst was cross-linked onto the matrix with 1% glutaraldehyde. The effects of various parameters, molar ratio of ferulic acid to isopropyl alcohol (25 mM : 100 mM), concentration of biocatalyst (2.5-20 mg/mL), molecular sieves (25-250 mg/mL), and various salt ions, were studied consecutively as a function of percent esterification. Immobilized lipase at 25 mg/mL showed maximum esterification (~84%) of ferulic acid and isopropanol at a molar ratio of 25 mM : 100 mM, respectively, in DMSO at 45°C in 3 h under shaking (150 rpm).
CONCLUSIONS:
To overcome the inhibitory effect of water (a byproduct) if any, in the reaction mixture, molecular sieves (3 Å × 1.5 mm; 100 mg/mL) were added to the reaction mixture to promote the forward reaction.
Salt ions like Ca(2+), Cd(2+), and Fe(2+) enhanced the activity of immobilized biocatalyst while a few ions like Co(2+), Zn(2+), Mg(2+), Mn(2+), Al(3+), and Na(+) had mild inhibitory effect. Approximately,
one third of total decrease in the esterification efficacy was observed after the 5th repetitive cycle of esterification. |
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