Different phyllosilicates as supports for lipase immobilisation

Abstract

The aim of this work was to determine the enzymatic activities resulting from the adsorption of Rhizomucor miehei lipase (RML) and Candida cylindracea lipase (CCL) onto three different phyllosilicates (sepiolite, palygorskite and montmorillonite), comparing the resultant activities with those obtained following similar immobilisation technique on a widely used resin (Duolite A-568). Due to the different adsorption mechanisms produced, different derivatives with higher hydrolytic activities can be obtained. Comparing the clays tested, the results showed that, in comparison with the laminar silicate (montmorillonite sample) and Duolite A-568 (spherical particles), fibrous materials (palygorskite and sepiolite) resulted in derivatives with higher hydrolytic activities in the hydrolysis of different ethyl esters. Moreover, according to the data obtained with the electrophoresis, the selectivity of immobilisation for RML in the case of fibrous silicates was optimal. As a conclusion, and according to the activities and selectivities measured, at least two out of the four studied materials (sepiolite and palygorskite) would be useful as supports for immobilisation for proteins of relatively low molecular weight (such as RML) for further use in biotransformations, while for C. cylindracea the immobilisation onto duolite rendered a derivative specially active in the hydrolysis of ethyl formiate (esterasic activity).