Importance de la forme cristalline de l'acétate de cortisone pour sa déshydrogénation en C-1 par Arthrobacter simplex

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Abstract
C-1 dehydrogenation of cortisone acetate by Arthrobacter simplex has been studied in two of its crystalline forms (II and IV). Primarily, transformation of crystalline form in aqueous medium has been studied (phosphate buffer and bacterial culture). In aqueous medium only form IV is stable and dehydrogenated, whatever the conditions of bioconversion. Form II goes to form IV in phosphate buffer but it is stable in bacterial culture. It is dehydrogenated by washed bacteria but not by bacterial culture. Tween 80 does not influence the transformation of crystalline forms. On the other hand, solubilities of the crystalline forms do not change much (phosphate buffer and bacterial culture). These facts suggest the existence of "association" phenomena between colloids in the culture medium and cortisone acetate. This "association" would prevent the dehydrogenation only in the case of form II. This hypothesis is supported by the favorable action of Tween 80 on dehydrogenation of form II in the bacterial culture.

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