Different phyllosilicates as supports for lipase immobilisation

Citation
Ie. De Fuentes et al., Different phyllosilicates as supports for lipase immobilisation, J MOL CAT B, 11(4-6), 2001, pp. 657-663
Citations number
24
Categorie Soggetti
Physical Chemistry/Chemical Physics
Journal title
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
ISSN journal
13811177 → ACNP
Volume
11
Issue
4-6
Year of publication
2001
Pages
657 - 663
Database
ISI
SICI code
1381-1177(20010122)11:4-6<657:DPASFL>2.0.ZU;2-U
Abstract
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.