Lipolytic activity was assayed in samples of Antarctic krill frozen in different conditions and in its liquid digesta with synthetic (tributylglycerol, esters of 2-naphtol and fatty acids C3, C9 , C14 and C18 ) and natural (olive oil) substrates. It was testified that the lipolytic activity is several-fold higher in the crustaceans with high food intake than in those with an empty digestive tract. Krill lipases show higher activity against esters of unsaturated fatty acids that against analogous derivatives of saturated ones and 10-fold higher affinity tributylglycerol (Km = 1.12 mM). Their maximal activity is at pH 6.4 and 37°C. E. superba lipases preserve total activity up to 35°C for 45 minutes, and are completely inactivated at 55°C for 5 minutes. Prevailing part of lipolytic activity is present in krill cephalothorax, however, extracts from krill abdomen also display a marked activity. Krill lipases are probably resistant to an attack of crustacean's proteinases.
Kinetic resolution of (R)- and (S)-mandelic acid by its transesterification with vinyl acetate catalysed by Burholderia cepacia lipase has been studied. The influence of the initial substrate concentration on the kinetics of process has been investigated. A modified ping-pong bi-bi model of enzymatic transesterification of (S)-mandelic acid including substrate inhibition has been developed. The values of kinetic parameters of the model have been estimated. We have shown that the inhibition effect revealed over a certain threshold limit value of the initial concentration of substrate.