Poor H
2
O
2
...
Poor H
2
O
2
-resistance by enzymes is a key bottleneck in the epoxidation process of oil by enzymatic methods. In this study, the stability of three lipases, from Aspergillus oryzae lipase (AOL), Aspergillus fumigatus lipase B (AflB), and marine Janibacter (MAJ1), in the presence of H
2
O
2
was evaluated in different types of natural deep eutectic solvents (NADES). This stability was strengthened significantly in the NADES compared to the buffer. Specifically, AOL retained 84.7% of its initial activity in the presence of choline chloride/sorbitol (1:1 M ratio) and 3 mol L
−1
H
2
O
2
after 24 h incubation at 40°C. In addition, the two-phase epoxidation process was optimized with AOL in ChCl/sorbitol to reach up to 96.8% conversion under the optimized conditions (molar ratio of octanoic acid/H
2
O
2
/C=C-bonds = 0.3:1.5:1, enzyme loading of 15 U g
−1
of soybean oil, ChCl/sorbitol content of 70.0% of the weight of hydrophilic phase, and reaction temperature of 50°C). Moreover, the lipase dispersed in NADES retained approximately 66% of its initial activity after being used for seven batch cycles. Overall, NADES-based enzymatic epoxidation is a feasible and promising strategy for the synthesis of epoxidized oils.
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