Z. Ujang et Am. Vaidya, STEPPED WATER ACTIVITY CONTROL FOR EFFICIENT ENZYMATIC INTERESTERIFICATION, Applied microbiology and biotechnology, 50(3), 1998, pp. 318-322
The benefits of controlling water activity, a(w), during enzymatically
catalysed synthesis reactions? such as reverse-hydrolytic reactions p
romoted by lipases, are now well recognized. Numerous techniques for c
ontrolling a(w) in the laboratory and their implementation in continuo
us reactors have been discussed in the published literature. However,
in enzymatic interesterification reactions, such as acidolysis and tra
nsesterification, it is not appropriate merely to maintain the a(w) of
the reaction system at one value since the two stages of the reaction
, namely the cleavage of the original acyl bond and the formation of a
new one, are best carried out at different levels of water activity -
the former at a high a(w) and the latter at a lower one. The use of a
continuous packed-bed hollow-fibre reactor has been described in this
article for carrying out solvent-free acidolysis of ethyl laurate wit
h octanoic acid with in situ a(w) control, using air that has been pre
-equilibrated with saturated salt solutions to the desired a(w). At a
single optimum(a(w) = 0.54), the highest steady-state conversion to et
hyl octanoate was 32%. However, it is possible to obtain a steady-stat
e conversion of 46% by operating the reactor with a step change in the
water activity, from an initial value of unity to 0.23.