Biotechnology Letters, Vol.25, No.1, 67-72, 2003
Enhanced hydantoinase and N-carbamoylase activity on immobilisation of Agrobacterium tumefaciens
Cell extracts of Agrobacterium tumefaciens, immobilised in calcium alginate beads, had a 7-fold increase in N-carbamoylase (N-carbamylamino acid amidohydrolase E. C. 3.5.1) activity on reaction with N-carbamylglycine. The hydantoinase (dihydropyrimidinase E. C. 3.5.2.2) and N-carbamoylase activities remained stable over 4 weeks storage at 4degreesC relative to the non-immobilised enzymes, with the hydantoinase activity showing a 5-fold increase in activity relative to the non-immobilised hydantoinase. The pH optima of the immobilised hydantoinase and N-carbamoylase enzymes decreased to pH 7 and pH 8, respectively. The temperature optimum remained at 40 C for the N-carbamoylase enzyme while the hydantoinase activity was optimal at 50degreesC.