CATALYTIC BEHAVIOR OF PSEUDOMONAS-CEPACIA LIPASE IN W O MICROEMULSIONS/

The activity of purified Pseudomonas cepacia lipase has been investiga ted in esterification reactions of various aliphatic alcohols with nat ural fatty acids. The reactions were carried out in microemulsions for med in isooctane by bis-(2-ethylhexyl)sulfosuccinate sodium salt (AOT) . Kinetic studies showed that the reaction follows a ping-pong bi-bi m echanism with inhibition by both substrates. The apparent kinetic para meters of the reaction were found to be K-m octanol = 310 mM, K-m laur ic acid = 78 mM, and V-max = 250 mu mol min(-1) mg(-1). The same syste m was used for the synthesis of mono- and diglycerides from glycerol a nd lauric acid, which was successful at very low w(o) values. The cata lytic behavior of P. cepacia lipase was also studied in esterification reactions performed in a nonionic microemulsion system formulated by tetraethyleneglycoldodecylether (C(12)E(4)). The optimum activity was found at about w(o) = 8. The apparent values of V-max app and K-m app for octanol were calculated and found to be 100 mu mol min(-1) mg(-1) and 76 mM, respectively. (C) 1995 John Wiley and Sons, Inc.