| Abstract: | Lipase-catalyzed interesterification between fish oil and medium-chain TAG has been investigated in a packedbed reactor with
a commercially immobilized enzyme. The enzyme, a Thermomyces lanuginosa lipase immobilized on silica by granulation (lipozyme TL IM; Novozymes A/S, Bagsvaerd, Denmark), has recently been developed
for fat modification. This study focuses on the new characteristics of the lipase in a packed-bed reactor when applied to
interesterification of TAG. The degree of reaction was strongly related to the flow rate (residence time) and temperature,
whereas formation of hydrolysis by-products (DAG and FFA) were only slightly affected by reaction conditions. The degree of
reaction reached equilibrium at 30–40 min residence time, and the most suitable temperature was 60°C or higher with respect
to the maximal degree of reaction. The lipase was stable in a 2-wk continuous operation without adjustment of water content
or activity of the column and the substrate mixture. |
