Purification and characterization of thermostable D-hydantoinase from Bacillus thermocatenulatus GH-2

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A thermostable D-hydantoinase was isolated from thermophilic Bacillus thermoatenalatus GH-2 and purified to homogeneity by using immunoaffinity chromatography. The molecular mass of the enzyme was determined to be about 230 kDa, and a value of 56 kDa was obtained as a molecular mass of the subunit on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, implying that oligomeric structure of the enzyme is tetrameric. Isoelectric pH of the enzyme was found to be approx 4.3. The enzyme required Mn2+ for the activity and exhibited its highest activity with phenylhydantoin as a substrate. The optimal pH and temperature for catalytic activity were about 7.5 and 65 degrees C, respectively. The half-life of the enzyme was estimated to be about 45 min at 80 degrees C.
Publisher
HUMANA PRESS INC
Issue Date
1999-01
Language
English
Article Type
Article
Keywords

MICROBIAL TRANSFORMATION; AMINO-ACIDS; STEAROTHERMOPHILUS SD-1; ENZYME; MICROORGANISMS; EXPRESSION; CLONING; GENE

Citation

APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, v.81, no.1, pp.53 - 65

ISSN
0273-2289
URI
http://hdl.handle.net/10203/71449
Appears in Collection
BS-Journal Papers(저널논문)
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