Compared esterification kinetics of the lipase from Burkholderia cepacia either free or encapsulated in a silica aerogel

S. Maury , P. Buisson (1) , A. Perrard (1) , A.C. Pierre (1)

1 IRC - Institut de recherches sur la catalyse

This paper presents an exptl. comparison of the kinetics of esterification catalyzed with the lipase from Burkholderia cepacia, either free, or encapsulated in a silica aerogel dried by the supercrit. CO2 method. The operational characteristics, in terms of pre-equilibration at given water thermodn. activity aw, mass of enzyme in the gel, size of aerogel particles, are presented. The kinetic model known as Bi-Bi Ping Pong with inhibition by both substrates has been found to fit relatively well with the exptl. results, except when both substrate concns. were high with the encapsulated enzyme. All kinetics consts. were found to be increased by aerogel encapsulation. In particular Vmax was increased by a factor of the order of 10 per mg of enzyme.

Domaines: Catalyse

S. Maury, P. Buisson, A. Perrard, A.C. Pierre. Compared esterification kinetics of the lipase from Burkholderia cepacia either free or encapsulated in a silica aerogel. Journal of Molecular Catalysis B: Enzymatic, 2005, 32 (5-6), pp.193-203. ⟨hal-00016941⟩