Abstract

Immobilizing enzymes on solid supports brings many advantages to enzymes’ industrial applications but is technically challenging. For lipases catalyzing the oil/water biphasic reactions, finding a suitable support that can position the enzyme at the interface between the oil phase and the water phase is difficult. Here we report covalent immobilization of SMG1, a monoacylglycerol (MAG) and diacylglycerol (DAG)-specific lipase, on hydrogel microparticles (HMPs) for biosynthesis of partial glycerides (a mixture of MAGs and DAGs) as a type of functional oil (a.k.a. healthy oil) ^[1]. Compared with covalent immobilization on epoxy-activated resin SEPLITE ®LX-1000EP, HMP-supported immobilization increased the hydrolytic activity of SMG1 in solutions of pH values that deviated from the optimal and high temperatures. In the esterification reaction where oleic acid is condensed with glycerol to form partial glycerides, the SMG1-HMP complex retained the catalytic activity and product distribution similar to that of the free SMG1. The SMG1-HMP complex contains both hydrophobic and hydrophilic islets, which create a microenvironment for the enzyme, oleic acid, and glycerol, manifesting as an interfacial phase between the oil and water layers ^[2]. Taken together, this work presents the use of HMPs as a support for the covalent immobilization of the lipase SMG1, the formation of an interfacial enzyme-contained phase for triphasic biocatalysis, and the potential use in the production of partial glycerides toward functional oil to combat obesity.

Reference:

1. Lee Y Y, Tang T K., Critical reviews in food science and nutrition, 2020, 60, 2509-2525.
2. Daly A C, Riley L., Nature Reviews Materials, 2020, 20-43