Interfacial engineering in lipase-catalyzed synthesis of functional lipids: Mechanisms, strategies, and prospects

The regulation of multiphase interfacial reactions is a central challenge in heterogeneous catalysis, where interfacial physicochemical properties govern reaction efficiency and selectivity. Lipase-catalyzed lipid transformations represent a prototypical model for biocatalysis at soft interfaces. Lipase activity is intrinsically dependent on lipid-water interfaces, where interfacial activation via lid-domain rearrangement and dynamic redistribution of enzymes, substrates, and products introduce regulatory complexity beyond homogeneous enzymatic systems. Especially in functional and structured lipid synthesis, catalytic performance is often limited by interface-induced deactivation, mass transfer constraints, and side reactions such as acyl migration. This review summarizes recent advances in interfacial regulation strategies, focusing on how interfacial microenvironments govern lipase catalytic behavior, providing mechanistic insights for the rational design of advanced lipase-based catalytic systems.