Modeling and optimization of phospholipase A₁-catalyzed hydrolysis of phosphatidylcholine using response surface methodology for lysophosphatidylcholine production.
Modeling the phospholipase A1 (PLA1 )-catalyzed partial hydrolysis of soy phosphatidylcholine (PC) in hexane for the production of lysophosphatidylcholine (LPC) and optimizing the reaction conditions using response surface methodology were described. The reaction was performed with 4 g of PC in a stirred batch reactor using a commercial PLA1 (Lecitase Ultra) as the biocatalyst. The effects of temperature, reaction time, water content, and enzyme loading on LPC and glycerylphosphorylcholine (GPC) content in the reaction products were elucidated using the models established. Optimal reaction conditions for maximizing the LPC content while suppressing acyl migration, which causes GPC formation, were as follows: temperature, 60°C; reaction time, 3 h; water content, 10% of PC; and enzyme loading, 1% of PC. When the reaction was conducted with 40 g of PC under these conditions, the reaction products contained 83.7 mol % LPC and were free of GPC. LPC had a higher total unsaturated fatty acid content than original PC had and was mainly composed of linoleic acid (78.0 mol % of the total fatty acids).
Dept. of Food Science and Technology, Chung-Ang University, Anseong, 456-756, Republic of Korea.
Chang Wan
CW
Lim
Byung Hee
BH
Kim
In-Hwan
IH
Kim
Moon-Won
MW
Lee
D000704:Analysis of Variance; D019149:Bioreactors; D005656:Fungal Proteins / Q000378:metabolism; D006868:Hydrolysis; D008244:Lysophosphatidylcholines / Q000032:analysis / Q000378:metabolism*; D010713:Phosphatidylcholines / Q000378:metabolism*; D054466:Phospholipases A1 / Q000378:metabolism*; D012107:Research Design; D013025:Glycine max / Q000737:chemistry; D013696:Temperature
D005656:Fungal Proteins; D008244:Lysophosphatidylcholines; D010713:Phosphatidylcholines; D054466:Phospholipases A1
acyl migration; hydrolysis; lysophosphatidylcholine; phospholipase A1; response surface methodology