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 Saha, B C Articles by Zeikus, J G Search for Related Content PubMed PubMed Citation Articles by Saha, B C Articles by Zeikus, J G Agricola Articles by Saha, B C Articles by Zeikus, J G

 Previous Article  |  Next Article 

Appl Environ Microbiol. 1990 September; 56(9): 2941-2943

Characterization of thermostable cyclodextrinase from Clostridium thermohydrosulfuricum 39E.

Michigan Biotechnology Institute, Lansing 48909.

ABSTRACT

Clostridium thermohydrosulfuricum 39E produced a cell-bound cyclodextrin (CD)-degrading enzyme (cyclodextrinase). It was partially purified 205-fold (specific activity, 14.5 U/mg of protein) by solubilizing with Triton X-100, ammonium sulfate treatment, and DEAE-Sepharose CL-6B column chromatography. The enzyme activity was found to be stable at pH 5.5 and 60 degrees C and optimally active at pH 6.0 and 65 degrees C. The enzyme preparation hydrolyzed CDs, with alpha-CD greater than beta-CD greater than gamma-CD, and displayed a putative multiple attack pattern. The enzyme activity was inhibited by p-chloromercuribenzoate but not by N-bromosuccinimide.

This article has been cited by other articles:

• Hashimoto, Y., Yamamoto, T., Fujiwara, S., Takagi, M., Imanaka, T. (2001). Extracellular Synthesis, Specific Recognition, and Intracellular Degradation of Cyclomaltodextrins by the Hyperthermophilic Archaeon Thermococcus sp. Strain B1001. J. Bacteriol. 183: 5050-5057 [Abstract] [Full Text]