Source:http://linkedlifedata.com/resource/pubmed/id/15304782
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
2004-8-12
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| pubmed:abstractText |
A thermostable D-hydantoinase was isolated from thermophilic Bacillus thermocatenulatus 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.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:status |
PubMed-not-MEDLINE
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| pubmed:month |
Jul
|
| pubmed:issn |
0273-2289
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
81
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
53-65
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| pubmed:year |
1999
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| pubmed:articleTitle |
Purification and characterization of thermostable D-hydantoinase from Bacillus thermocatenulatus GH-2.
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| pubmed:affiliation |
Department of Biological Sciences, Korea Advanced Institute of Science and Technology, 373-1 Kusung-dong Yusung-gu, Taejon 305-701 Korea.
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| pubmed:publicationType |
Journal Article
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