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.
Pfitzner
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Lehrstuhl für Pharmazeutische Biologie, Universität München, Federal Republic of Germany.
Zenk
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