Immobilization of lipase in cage-type mesoporous organosilicas via covalent bonding and crosslinking》.pdfVIP

Catalysis Today 243 (2015) 173–183 Contents lists available at ScienceDirect Catalysis Today j o u r n a l h o me p a ge : w w w. elsev /locate/cattod Immobilization of lipase in cage-type mesoporous organosilicas via covalent bonding and crosslinking Zhou Zhou, Frank Piepenbreier, V.R. Reddy Marthala, Karl Karbacher, Martin Hartmann ∗ Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen Catalysis Resource Center (ECRC), Egerlandstraße 3, 91058 Erlangen, Germany a r t i c l e i n f o a b s t r a c t Article history: Lipase from Thermomyces lanuginosus (TLL) was immobilized in cage-type mesoporous materials via two Received 9 June 2014 different protocols, viz. covalent bonding and cross-linking. The comparison between the biocatalysts Received in revised form 21 July 2014 generated by the two methods on both pure silica mesocellular siliceous foam (MCF) and cage-type Accepted 22 July 2014 large pore mesoporous organosilicas (PMOs) disclosed that cross-linking results in the immobilization Available online 18 September 2014 of a larger amount of TLL and reduced diffusion problems compared to covalent bonding. Benzene- bridged PMOs positively influence the activity of immobilized lipase due to the hydrophobic properties Keywords: of the surface. Furthermore, a transesterification reaction in organic solvent was carried out to verify Li