Synthesis of L-α-glycerylphosphorylcholine catalyzed by anion exchange resin-immobilized phospholipase A1 in aqueous phase

L-α-Glycerylphosphorylcholine (GPC) is a key biosynthetic precursor of the human neurotransmitter acetylcholine with multiple biological functions. Currently, the enzymatic preparation of GPC is limited by the poor stability, low reusability and unsatisfactory catalytic efficiency of free phospholipase A 1 (PLA1). To address these limitations, this study constructed aqueous catalytic system using anion-exchange acrylic resin LXTE-902 immobilized PLA1 as the biocatalyst and egg yolk lecithin (PC) as the substrate for GPC preparation. The results indicated that LXTE-902 exhibited excellent immobilization performance for PLA1, with an immobilization capacity of 65.9 mg/g. Under optimized conditions, the immobilized PLA1 efficiently catalyzed PC hydrolysis within 1 h, achieving a high GPC yield of 93.7%. A facile solvent extraction and precipitation purification method was further developed to efficiently separate free fatty acids from the reaction system, affording high-purity GPC with a purity of 92%. Compared with free PLA1, the immobilized biocatalyst possessed superior storage stability, pH tolerance and solvent tolerance, and retained a GPC yield of 40% after seven reuse cycles. This work demonstrates that LXTE-902-immobilized PLA1 is an efficient, stable and recyclable biocatalyst. The proposed enzymatic strategy provides a promising technical reference for industrial-scale production of high-purity GPC.