Immobilized enzymes active toward macromolecular substrates: biocatalyc matrices for pectic substance degradation
1994
Dinnella, C. | Lanzarini, G. | Laus, M. | Zannoni, M. (Bologna Univ. (Italy). Dept. of Industrial Chemistry and Materials)
An endo-pectinlyase present in a commercial mixture was immobilized on EUDRAGIT L100-55, a co-polymer which is reversibly soluble-insoluble depending on the medium pH. The enzymatic activities of biocatalysts obtained by activating the polymer either with water-soluble carbodiimide or by simple adsorption, were compared. The biocatalyst obtained by adsorption showed an enzymatic activity higher (500 Enzymatic Units per gram) than that obtained using the activated polymer (50 Enzymatic Units per gram). Moreover, the activating agent use does not appear necessary to stabilize the interaction between the enzyme and the carrier. The immobilization procedure did not alter the main biochemical parameters of the immobilized enzyme with respect to its free form, appreciably enhancing its stability at 25 degrees Celsius. In addition, the fresh vegetable tissue softening ability of the biocatalyst obtained was tested. Preliminary results as to the use of double shell microspheres in order to overcome unwanted co-precipitation phenomena, related to the removal of the immobilized enzyme from the reaction mixture by polymer insolubilization, are reported.
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Эту запись предоставил University of Liège