An endo-pectinlyase present in a commercial mixture was immobilized on
EUDRAGIT L100-55, a polymer which is reversibly soluble-insoluble dep
ending on the pH of the medium. The enzymic activities of biocatalytic
matrices, obtained by pre-activating the polymer either with water-so
luble carbodiimide or by simple adsorption, were compared The biocatal
yst obtained by adsorption showed an enzymic activity higher (500 E.U.
g(-1)) than that obtained using the activated polymer (50 E.U. g(-1))
. Moreover, the activating agent did not seem to be necessary in order
to stabilize the interaction between carrier and protein. In fact abo
ut 80% of the initial activity was detectable on both matrices after r
epeated washings with NaCl 0.2 M, The immobilization procedure did not
alter the main biochemical parameters of the immobilized enzyme with
respect to its native form and appreciably enhanced its stability in t
he temperature range 25-45 degrees C.