1976 Volume 22 Issue 1 Pages 25-33
The enzymatic transformation of cortisol with Bacillus cereus was examined in the presence of some redox agents and enzyme inhibitors. At the early phases of fermentation, the enzymic 1, 2-dehydrogenation reaction of cortisol was highly accelerated in the presence of oxidized glutathione. Thereafter, the enzymic reduction of the 20-keto group of cortisol and prednisolone was noticeably enhanced. In the presence of reduced glutathione, prednisolone was quantitatively converted to the 20β-hydroxy derivative. The bioconversion of cortisol to prednisolone, 20β-hydroxycortisol, and 20β-hydroxyprednisolone was also activated in the presence of azide and cyanide. With iodoacetate, the 1, 2-dehydrogenation reaction was promoted while the 20-keto reduction was markedly repressed.
Pretreatment of the bacterial cells with various C19 and C21 steroids as well as with cholesterol affected the transformation pattern in different manners. The 1, 2-dehydrogenation reaction of cortisol was considerably induced when the cells were pretreated with Δ1-dehydroprogesterone, Δ1, 4-androstadienedione, and Δ1-dehydrotestosterone.