The aim of this work was to determine the enzymatic activities resulting fr
om 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 obtain
ed following similar immobilisation technique on a widely used resin (Duoli
te A-568). Due to the different adsorption mechanisms produced, different d
erivatives with higher hydrolytic activities can be obtained. Comparing the
clays tested, the results showed that, in comparison with the laminar sili
cate (montmorillonite sample) and Duolite A-568 (spherical particles), fibr
ous materials (palygorskite and sepiolite) resulted in derivatives with hig
her hydrolytic activities in the hydrolysis of different ethyl esters. More
over, according to the data obtained with the electrophoresis, the selectiv
ity of immobilisation for RML in the case of fibrous silicates was optimal.
As a conclusion, and according to the activities and selectivities measure
d, at least two out of the four studied materials (sepiolite and palygorski
te) would be useful as supports for immobilisation for proteins of relative
ly low molecular weight (such as RML) for further use in biotransformations
, while for C. cylindracea the immobilisation onto duolite rendered a deriv
ative specially active in the hydrolysis of ethyl formiate (esterasic activ
ity). (C) 2001 Elsevier Science B.V. All rights reserved.