Immobilized Talaromyces leycettanus phospholipase A1 as a reusable biocatalyst for l-α-glycerylphosphorylcholine preparation from phosphatidylcholine

l-α-Glycerylphosphorylcholine (l-α-GPC), a cognitive enhancer, can be prepared via phospholipase A₁ (PLA₁)-catalyzed hydrolysis of soy phosphatidylcholine (PC). Quara LowP (QLP), a commercial liquid PLA₁ from Talaromyces leycettanus, has not yet been used for the preparation of l-α-GPC. This study aimed to establish the optimal conditions for the immobilized QLP-catalyzed hydrolysis of soy PC to prepare l-α-GPC and evaluate the reusability of the enzyme under these conditions. The immobilized QLP was prepared via physical adsorption onto Lewatit VP OC (LVO) 1600. The reaction was performed in n-hexane–water biphasic media in a stirred-batch reactor, achieving complete conversion to l-α-GPC. Optimal conditions included a temperature of 55°C, a soy PC-to-water molar ratio of 1:10, an enzyme loading (based on the protein quantity) of 10 mg/g soy PC, and a reaction time of 12 h. Gradual morphological alterations on the surface of the immobilized QLP, such as the formation of cracks and dents, were observed via scanning electron microscopy over six successive reuse cycles. Nevertheless, the immobilized QLP achieved complete conversion to l-α-GPC in its first reuse cycle under the optimal conditions up to the fifth cycle of reuse, with the extension of the reaction time to 60 h. These findings suggest that the LVO 1600-immobilized QLP is a promising and reusable biocatalyst for the hydrolysis of soy PC to prepare l-α-GPC.