Artificial antibody-antigen-mediated lipase immobilization via a simplified affinity recognition strategy for biocatalytic flavor ester synthesis through transesterification

Flavor esters are extensively used in food and cosmetic industries, yet their sustainable production remains challenging. This study developed a lipase bioreactor through artificial antibody-antigen-mediated immobilization for biocatalytic flavor ester synthesis via transesterification. Artificial antigens were prepared by lipase modification with p -nitrobenzaldehyde, while artificial antibodies were synthesized using 2-(4-nitrophenyl)-1,3-dioxolane (acetal-protected p -nitrobenzaldehyde analogue) as template molecules. These components self-assembled into immobilized lipase with 82.24 ± 0.13% immobilization efficiency, 17.59 ± 0.12 mg/g capacity, and 8.81 ± 0.27 U/mg specific activity. Integrating molecular simulations with acyl donor screening, the bioreactor achieved 97.18 ± 0.93% yield for cinnamyl acetate synthesis from cinnamyl alcohol and vinyl acetate. The system demonstrated exceptional continuous catalysis and scalability, confirming industrial translation potential. Successful synthesis of cinnamyl butyrate (86.25 ± 3.34%) and benzyl acetate (90.68 ± 2.25%) further established its versatility as a platform for diverse flavor ester production.