Increased stability of galactosyltransferase on immobilization.

Abstract

The stability of galactosyltransferase was greatly enhanced on immobilization. The immobilized enzyme was demonstrated to be insensitive to mechanical stirring for several hours, whereas its soluble counterpart was totally inactivated in less than 60 min under the same conditions. Immobilization also conferred increased thermostability to the enzyme. The Arrhenius energy of inactivation was raised from 13 kcal/mol for the soluble enzyme to 30 kcal/mol for the immobilized protein. The gel-bound enzyme could be stored at 4 degrees C for over 10 months without apparent loss of activity.