Purification and Characterization of Glycerol 3-Phosphate Dehydrogenase from Two Types of Acidiphilium sp

Takashi Hatta, Kenji Inagaki, Tsuyoshi Sugio, Noriaki Kishimoto, Tatsuo Tano

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Acidiphilium sp. 63 and 24R, which were isolated from strongly and weakly acidic environments, grew well on glycerol. Both glycerol kinase and glycerol 3-phosphate dehydrogenase (G3PDH) were induced during growth on glycerol. After centrifugation of the crude extracts at 100, 000 × g for 60 min, the G3PDH activity in strain 63 was found in the precipitate, on the other hand, 80 % of that in strain 24R was found in the supernatant. We solubilized the G3PDH from strains 63 and 24R with 0.1 % Brij 58, and both enzymes were purified to homogeneity. When a detergent was removed from these enzymes with cold aqueous 90% acetone, the activities were reduced to 11% and 28%, and were restored to about 55% of the original activities on addition of 0.1% Brij 58. By sonication with phospholipid, the 63-G3PDH activity was restored very well. Both purified enzymes have a molecular weight of 108, 000 and their coenzymes were FAD. These enzymes from strain 63 and 24R had a Km of 0.38 and 1.3 mM for DL-glycerol 3-phosphate and the optimal pHs of these enzymes were 7.0 and 8.8, respectively.

Original languageEnglish
Pages (from-to)651-658
Number of pages8
JournalAgricultural and Biological Chemistry
Issue number3
Publication statusPublished - 1989


ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

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