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. 1990 Sep;56(9):2941–2943. doi: 10.1128/aem.56.9.2941-2943.1990

Characterization of thermostable cyclodextrinase from Clostridium thermohydrosulfuricum 39E.

B C Saha 1, J G Zeikus 1
PMCID: PMC184873  PMID: 2275540

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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