This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Igarashi, T Articles by Takamori, K Search for Related Content PubMed PubMed Citation Articles by Igarashi, T Articles by Takamori, K

 Previous Article  |  Next Article 

Infect Immun. 1987 December; 55(12): 3001-3005

Purification and characterization of levanase from Actinomyces viscosus ATCC 19246.

Department of Oral Microbiology, Showa University School of Dentistry, Tokyo, Japan.

ABSTRACT

The extracellular levanase of Actinomyces viscosus ATCC 19246 was purified about 3,701-fold in 11% yield from the bacterial culture supernatant by means of ammonium sulfate precipitation, followed by DE52 column chromatography, Sephadex G-100 gel filtration, hydroxylapatite column chromatography, and Bio-Gel A 1.5m gel filtration. The molecular weight of the enzyme was estimated to be 89,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme was optimally reactive at pH 6.0 and at 45 degrees C. The activity was inhibited by MnCl2, BaCl2, FeCl3, ZnCl2, HgCl2, and EDTA at a final concentration of 1 mM. The inhibition by EDTA was recovered by adding CaCl2 or MgCl2. The enzyme specifically hydrolyzed levan, but not sucrose, raffinose, melezitose, inulin, and dextran. These results indicate that the purified enzyme is specific for fructan (i.e., levan), which mainly consists of beta-(2,6) linkages.

This article has been cited by other articles:

• Bergeron, L. J., Burne, R. A. (2001). Roles of Fructosyltransferase and Levanase-Sucrase of Actinomyces naeslundii in Fructan and Sucrose Metabolism. Infect. Immun. 69: 5395-5402 [Abstract] [Full Text]