Effect of acyl migration in Lipozyme TL IM-catalyzed interesterification using a triacylglycerol model system
Lipase-(Lipozyme TL IM) catalyzed interesterification of triacylglycerols was studied at water activities (a(w)) from 0.22 to 0.8. The substrates trilaurin (LLL) and 1,3-palmitin-2-olein (POP) were used in equimolar amounts to facilitate separate measurements of the interesterification in the sn-1,3 positions and changes in the fatty acid (FA) composition in the sn-2 position. The reaction at a(w)
