Immobilization of some hydrolases on polymethacrylate by the method of reactive esters

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Abstract
The immobilization of chymotrypsin (EC 3.4.4.5), papain (EC 3.4.4.10), α-amylase (EC 3.2.1.1), amyloglucosidase (EC 3.2.1.3), and of a technical pectolytic enzyme on various reactive polymethacrylate esters (Ostion KM) was examined and compared with the immobilization of the same enzymes on carboxymethyl-cellulose. There is no difference in the individual reactive esters (2,4-dinitrophenyl, N-hydroxysuccinimidyl, ethyl-1-hydroxyacetyl) when enzymes reacting fast (papain, chymotrypsin) are immobilized. The ethyl-1-hydroxyacetyl ester of the support is most suitable for slowly reacting enzymes. The reaction does not proceed at pH-values lower than 7.5. The specific activity of immobilized amylolytic and pectolytic enzymes decreases with the increasing pH because of inactivation of the enzyme.

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