Affiliation: | (1) State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, 1800 Lihu Road, Wuxi, 214122, Jiangsu, People’s Republic of China |
Abstract: | 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. |