Immobilization of strictosidine synthase from Catharanthus cell cultures and preparative synthesis of strictosidine.

Strictosidine synthase was partially purified from Catharanthus roseus cell suspension cultures and immobilized on CNBr-activated Sepharose. The immobilized enzyme exhibits a thermostability increased 300 fold over that of the soluble enzyme and catalyses exclusively the formation of the 3alpha(S)-isomer, strictosidine. Gram quantities of this biologically active glucoalkaloid, which hitherto had been difficult to synthesize and purify, were prepared.