Enzymatic Interesterification of Palm Stearin and Palm Olein Blend Catalyzed by sn-1,3-Specific Lipase: Interesterification Degree, Acyl Migration, and Physical Properties

Acyl migration of fatty acid at sn-2 is often observed alongside enzymatic interesterification (EIE), causing the loss lipase selectivity toward acyl group sn-1,3. In this study, an oil blend consisting palm stearin (PST) and olein (POL) was interesterified via a chemical (CIE) method using packed bed reactor. Characterization in terms triacylglycerol (TAG) compositions, distributions, solid fat content profiles performed. comparison to that CIE fats, EIE fats showed different modification effects on content. Under similar reaction conditions, degrees (IDs) were obtained according various ratios. Using same mass ratio substrates (POL/PST 9:1), time temperature affected ID change position. 46 min, 94.41% acquired, while 80 °C, degree 92.87%. with high exhibited lower crystallization rate than low migration. However, effect crystal polymorphism oxidative stability insignificant. Outcomes from study are meaningful for establishment theoretical basis controlled positional-specific catalyzed by sn-1,3-specific lipase.