Li_2024_Food.Chem_463_141075

In order to improve the esterification efficiency of the enzymatic synthesis of l-ascorbic acid palmitate, the substrate analogue imprinting of the Aspergillus niger lipase-catalyzed esterification process was studied. Oleic acid was selected as the imprinting molecule, oleic acid imprinting immobilized lipase was prepared at pH 8.0, 0.1 g oleic acid, 1.5 mL of 95 % ethanol, and 0.1 g Tween-20. Through solubilization and supersaturation of Vitamin C, the reaction concentration of Vitamin C reached 5.00 % (m/v) in dioxane with 93.99 % esterification rate and 110.72 g/L of product concentration. Moreover, the Vitamin C reaction concentration can reach 8.00 % by using staged substrate feeding, and the esterification rate and product concentration of esterification after 28 h was 156.34 g/L and 82.96 %. Besides, the imprinting-induced conformational changes in enzyme proteins was characterized by fluorescence and infrared spectroscopy. This method provides a pathway for enzymatic production of l-ascorbic acid palmitate.