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.
* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.