Co-immobilized pectinlyase and endocellulase on chitin and Nylon supports

Some factors influencing easy immobilization procedures on Nylon and chitin supports were optimized in terms of the highest activity of immobilized pe ctinlyase, using two experimental designs. Optimal procedures were applied to co-immobilized pectinlyase (P1, EC 4.2.2.3) and endocellulase (Cx, EC 3. 2.1.4), using a commercial enzyme but omitting preliminary purification ste ps. Purified enzyme solutions were not used. The kinetic characteristics of co-immobilized pectinlyase and endocellulase were assessed for both suppor ts. Chitin was more suitable for applications to fruit juice liquefaction b ecause both immobilized pectinlyase and endocellulase showed higher activit y at low pH and low temperature. Furthermore. the half-life of pectinlyase bound to chitin was higher than with Nylon (407 h against 19 h). The immobi lization procedure on chitin was not only inexpensive, but also very easy t o carry out so that the potential for industrial application is considerabl e. (C) 2000 Elsevier Science Ltd. All rights reserved.