Zhang_2024_Food.Chem_464_141709

The 2-arachidonoylglycerol enzymatic alcoholysis reaction model was established and kinetic parameters were calculated to explore the effects of solvent and water activity (a(w)) on the lipase positional selectivity and 2-monoacylglycerol acyl migration. Six rate constants (k(1)-k(6)) with the lowest mean square error were obtained using the particle swarm optimization algorithm, and the calculated molar concentration-time curves were well-fitted to the actual curves. As an indicator to characterize the positional selectivity of lipase, k(5)/k(3) was significantly associated with log P of solvent, which first increased and then decreased with the increase of a(w). The highest sn-1,3 selectivity of Lipozyme TL IM was found at the a(w) of 0.53. The changes of acyl migration with the solvent and a(w) in the enzymatic and non-catalytic systems showed a consistent law. This study provides theoretical support for the targeted synthesis of structural lipids and enzymatic production of diverse structural lipid products.