PURIFICATION AND CHARACTEIZATION OF (S)-TETRAHYDROBERBERINE OXIDASE FROM CULTURED COPTIS JAPONICA CELLS
(S)-Tetrahydroberberine (THB) oxidase was purified to homogeniety from cultured Coptis japonica cells by DEAE-Sepharose chromatography, gel filration, and HPLC.The enzyme catalysed the removal of four hydrogen atoms from one mol of (S)-THB and produced two mol of hydrogen peroxide and one mol of berberine in the presence of molecular oxygen.The purified enzyme had neither the yellow fluoresence characteristic of flavin derivatives nor an absorption spectrum showing the presence of haem.The enzyme had a M, of 58000 and consisted of two identical subunits of 28000 each.Key Word Index: Coptis japonica; Ranunculaceae; cultured cells; berberine; (S)-tetrahydroberberine; (S)-tetrahydroberberine oxidase
Biotransformation of tetrahydroberberine to berberine by enzymes prepared from cultured coptis japonica cells
Crude enzymes were extracted from cultured Coptis japonica cells producing large amounts of berberine. One of the enantiomers of tetrahydroberberine, (S)-(-)-tetrahydroberberine, was dehydrogenated to berberine by the enzyme system.