Thermostable D-hydantoinase from thermophilic Bacillus stearothermophilus SD-1 : characteristics of purified enzyme

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Title
Thermostable D-hydantoinase from thermophilic Bacillus stearothermophilus SD-1 : characteristics of purified enzyme
Author(s)
Seung Goo LeeDong Chul Lee; Seung Pyo Hong; Moon Hee Sung; H S Kim
Bibliographic Citation
Applied Microbiology and Biotechnology, vol. 43, no. 2, pp. 270-276
Publication Year
1995
Abstract
One thousand thermophiles isolated from soils were screened for hydantoinase and its thermostability. One thermophilic bacterium that showed the highest thermostability and activity of hydantoinase was identified to be Bacillus stearothermophilus SD-1 according to morphological and physiological characteristics. The hydantoinase of B. stearothermophilus SD-1 was purified to homogeneity via ammonium sulfate fractionation, anion-exchange chromatography, heat treatment, hydrophobic-interaction chromatography and preparative gel electrophoresis. The relative molecular mass of the hydantoinase was determined to be 126 kDa by gel-filtration chromatography, and a value of 54 kDa was obtained as a molecular mass of the subunit on analytical sodiumdodecylsulfate/polyacrylamide gel electrophoresis. The hydantoinase was strictly D-specific and metal-dependent. The optimal pH and temperature were about 8.0 and 65°C respectively, and the half-life of the D-hydantoinase was estimated to be 30 min at 80°C, indicating the most thermostable enzyme so far.
ISSN
0175-7598
Publisher
Springer
DOI
http://dx.doi.org/10.1007/BF00172823
Type
Article
Appears in Collections:
Synthetic Biology and Bioengineering Research Institute > 1. Journal Articles
Division of Biomedical Research > Personalized Genomic Medicine Research Center > 1. Journal Articles
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