Candida antartica lipase-catalyzed esterification for efficient partial acylglycerol synthesis in solvent-free
Shuo Zou1, Jiena Chen1, Yee-Ying Lee2
1JNU-UPM International Joint Laboratory on Plant Oil Processing and Safety, Department of Food Science and Engineering, Jinan University, Guangzhou, Guangdong 510632, China.
Abstract:
Partial acylglycerols are valued for their emulsifying and stabilizing properties, yet precise green synthesis remains challenging due to low yield and selectivity. This study aimed to elucidate the "lipase selectivity-substrate structure-product composition" relationship to enhance the yield of targeted partial acylglycerol. The results showed that lipase exhibited a greater selectivity towards fatty acids with shorter chain lengths and higher unsaturation. Hydroxyl donors also affected the esterification process, with the enzyme-acyl complex exhibiting selectivity towards hydroxyl donors as follows: glycerol > monoacylglycerol > diacylglycerol. Substrate ratio significantly influenced enzymatic reactions; a 10:1 ratio favored triacylglycerol formation (>80 %), while a 1:1 ratio produced > 90 % partial acylglycerols. Molecular docking simulations revealed that substrates primarily interacted with lipase through hydrogen bonding and hydrophobic interactions. A comprehensive understanding of lipase selectivity patterns could facilitate the design of more efficient reaction systems, enabling the conversion of basic lipid resources into desired high value-added products.
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