Purification and properties of an acidic β-glucosidase from Acidobacterium capsulatum

Noriaki Kishimoto, Kenji Inagaki, Tsuyoshi Sugio, Tatsuo Tano

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11 Citations (Scopus)


Acidobacterium capsulatum, an acidophilic, mesophilic and chemoorganotrophic bacterium, produced an inducible, acidic β-glucosidase in the cellobiose medium. The enzyme was successively purified 109 times by CM-Sepharose, Sephacryl S-200 chromatography and preparative discontinuous polyacrylamide gel electrophoresis. Polyacrylamide gel electrophoresis of the purified enzyme gave a single band at pH 4.3. The enzyme had an optimum pH of 3.0 and optimum reaction temperature of 55°C, being stable from pH 1.5 to 6.0 and at temperatures from 20 to 45°C. No activity was detected above pH 6.5 or above 65°C. The molecular weight of 90,000 was estimated by gel filtration and the enzyme had an isoelectric point of 7.0. The enzyme hydrolyzed aryl-β-glycosides and β-linked disaccharides.

Original languageEnglish
Pages (from-to)318-321
Number of pages4
JournalJournal of Fermentation and Bioengineering
Issue number5
Publication statusPublished - 1991

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology


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