Aqueous medium enzymatic preparation of l-alpha glycerylphosphorylcholine optimized by response surface methodology
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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.
KeywordsCentral composite rotatable design Glycerylphosphorylcholine Rhizopus chinensis lipase (Thermo 4S-3) Optimal Response surface methodology
The work is supported by Key Projects in the National Science & Technology Pillar Program during the Twelfth Five-Year Plan Period of China (Contract No: 2011BAD02B04) and Program for New Century Excellent Talents in University (NECT). The authors also thank the Testing & Analysis Center of Jiangnan University.
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