Acyl migration phenomenon of Sn-2-lysophosphatidylcholine(Sn-2-LPC) was confirmed through hydrolysis process analysis of phosphatidylcholine by phospholipase A1(Lecitase Ultra). Based on previous studies on the automatical acyl migration mechanism of monoglyceride, the automatical acyl migration mechanism of Sn-2-LPC in the acid and alkali conditions was speculated. Acyl migration directionalities of Sn-2-LPC and Sn-1-LPC were explored by HPLC-RID. It was found that acyl migration of Sn-2-LPC to Sn-1-LPC happened, while acyl migration of Sn-1-LPC was not present. Meanwhile, the inhibition mechanism of acyl migration of Sn-2-LPC through Al(OH)3, Zn(OH)2 and B(OH)3 was speculated by boric acid. The minimum dosages of Al(OH)3, Zn(OH)2 and B(OH)3 were determined as 0.97, 0.85 mg/mL and 0.72 mg/mL. A theoretical basis and data support for the synthesis of mixed acyl phospholipids and the explanation of biosynthetic pathway (lysophospholipid intermediate) of mixed acyl phospholipids were provided. |