Covalently immobilized lipase on aminoalkyl-, carboxy- and hydroxy-multi-wall carbon nanotubes in the enantioselective synthesis of Solketal esters.

Aiming at the preparation of efficient, stable on storage and recyclable nanobiocatalysts for enantioselective transesterification, alkaline lipase from Pseudomonas fluorescens was covalently immobilized (up to 8.5wt.%) on functionalized multi-wall carbon nanotubes (f-MWCNTs).

Immobilization of an integral membrane protein for biotechnological phenylacetaldehyde production.

Styrene oxide isomerase (SOI) has previously been shown to be an integral membrane protein performing a highly selective, hydrolytic ring opening reaction of epoxides to yield pure aldehydes. Earlier studies had also shown a high sensitivity of SOIs toward their product phenylacetaldehyde which caused an irreversible inhibition and finally complete loss of activity at higher aldehyde concentrations. Here we report on the covalent immobilization of a styrene oxide isomerase (SOI) on SBA-15 silica carriers.

Alkaline lipase from Pseudomonas fluorescens non-covalently immobilised on pristine versus oxidised multi-wall carbon nanotubes as efficient and recyclable catalytic systems in the synthesis of Solketal esters.

In order to produce effective and recyclable catalysts for enantioselective transesterification in the industrial applications, alkaline lipase from Pseudomonas fluorescens was non-covalently immobilised (ca. 6 wt%) on pristine multi-wall carbon nanotubes (MWCNTs) and oxidised MWCNTs (O-MWCNTs) using an adsorption technique. Mesoporous silica modified with n-octyl groups was used as a reference support.