Co-immobilized recombinant glycosyltransferases efficiently convert rebaudioside A to M in cascade

. Eventually, after 4 and 8 reused cycles, the co-immobilized enzymes retained 72.5% and 53.1% of their original activity, respectively, showing a high stability to minimize the total cost of enzymes and suggesting that the co-immobilized UGTs is of potentially signficant value for the production of Reb M.