Enzymatic trans- and interesterification processes

By fatty acid (A and B) specific lipase catalysed interesterification  

The kinetics of these reactions are important when planning such reactions. Simplistically, enzymatic trans- and interesterification reaction rates are defined by their degree of conversion (Sawamura, 1988). The degree of conversion is determined by measuring the distributional change of the target fatty acid that occurs in the reaction system, and is represented as 

The transesterification activity (Af.) can be defined as the product of k and the quotient of the amount of substrate (5) and the amount of enzyme (E) used. Therefore, Ae can be expressed as 

These equations may be generally used in following trans- and interesterification reactions. 

3-spedfic lipase catalysed interesterification reactions, Kyotani et al. (1988a) have provided elaborate kinetic models of the reactions using biphasic and microaqueous conditions. Four models were studied (a) first order kinetics (b) hydrolysis followed by resynthesis (c) reaction via the glyceride-enzyme complex (d) reactions via the acyl-enzyme complex. Details of the models are beyond the scope of this chapter. Interested readers are referred to Kyotani et al. (1988a) for an in-depth treatment of each model. For illustration purposes, the mathematical treatment of the simplest model is presented here. 

---