Acyl migration occurrence of palm olein during interesterification catalyzed by sn-1,3 specific lipase

Palm olein was enzymatically interesterified (EIE) using sn-1,3 specific lipase and the effect of different reaction conditions on the degree of acyl migration (AMD) was investigated. The AMD increased with the amount of lipase loaded, recording the highest AMD of 63.41% when 11% of lipase was added at 80 °C for 2 h. When the reaction time and temperature was further increased, the AMD remained constant at 100%, reaching a completely randomized interesterification. Post EIE, the triacylglycerol (TAG) molecular structures were modified and this contributed to the modification of the crystallization behaviour, solid fat content, and thermal properties of the interesterified products. Higher AMD promoted a random rearrangement of the TAG to obtain tri-saturated TAG and achieved a fast crystallization. Hence, the crystal microstructures were observed to be more uniform and was dominated with β′ crystals. The findings that were acquired in this study are meaningful for the establishment of a theoretical framework that can be used to monitor and control the AMD during an sn-1,3 specific lipase-catalyzed EIE.