Characterization of thermostable cyclodextrinase from Clostridium thermohydrosulfuricum 39E.

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.

journal_name

Appl Environ Microbiol

authors

Saha BC,Zeikus JG

doi

10.1128/AEM.56.9.2941-2943.1990

subject

Has Abstract

pub_date

1990-09-01 00:00:00

pages

2941-3

issue

9

eissn

0099-2240

issn

1098-5336

journal_volume

56

pub_type

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