Aqueous medium enzymatic preparation of <Emphasis Type="SmallCaps">l</Emphasis>-alpha glycerylphosphorylcholine optimized by response surface methodology

The ability of Rhizopus chinensis lipase (Thermo 4S-3) to catalyze the deacylation of l,2-diacyl-sn-glycero-3-phosphocholines (sn-1,2-PC) for l-alpha glycerylphosphorylcholine (l-α-GPC) preparation was investigated. Response surface methodology (RSM), based on a modified central composite rotatable design, was employed to examine the effects of substrate concentrations, temperature, enzyme loading, and dosage of CaCl₂ on the l-α-GPC yield. RSM analysis indicated good correlation between experimental and predicated values. The optimal condition was confirmed as follows: reaction time, 3.5 h; temperature, 43 °C; enzyme loading, 28.2 U mL⁻¹; substrate concentration, 51.5 mg mL⁻¹; and dosage of CaCl₂, 1.9 mg mL⁻¹. Under these conditions, the l-α-GPC yield increased by 96.8%, which was close to the amount predicted by the model.