Source:http://linkedlifedata.com/resource/pubmed/id/21421786
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
10
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| pubmed:dateCreated |
2011-5-12
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| pubmed:abstractText |
Enzymatic processes are useful for industrially important sugar production, and in vitro two-step isomerization has proven to be an efficient process in utilizing readily available sugar sources. A hypothetical uncharacterized protein encoded by ydaE of Bacillus licheniformis was found to have broad substrate specificities and has shown high catalytic efficiency on D-lyxose, suggesting that the enzyme is D-lyxose isomerase. Escherichia coli BL21 expressing the recombinant protein, of 19.5 kDa, showed higher activity at 40 to 45°C and pH 7.5 to 8.0 in the presence of 1.0 mM Mn²+. The apparent K(m) values for D-lyxose and D-mannose were 30.4 ± 0.7 mM and 26 ± 0.8 mM, respectively. The catalytic efficiency (k(cat)/K(m)) for lyxose (3.2 ± 0.1 mM?¹ s?¹) was higher than that for D-mannose (1.6 mM?¹ s?¹). The purified protein was applied to the bioproduction of D-lyxose and D-glucose from d-xylose and D-mannose, respectively, along with the thermostable xylose isomerase of Thermus thermophilus HB08. From an initial concentration of 10 mM D-lyxose and D-mannose, 3.7 mM and 3.8 mM D-lyxose and D-glucose, respectively, were produced by two-step isomerization. This two-step isomerization is an easy method for in vitro catalysis and can be applied to industrial production.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Coenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/Manganese,
http://linkedlifedata.com/resource/pubmed/chemical/Mannose,
http://linkedlifedata.com/resource/pubmed/chemical/Pentoses,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Xylose,
http://linkedlifedata.com/resource/pubmed/chemical/lyxose
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| pubmed:status |
MEDLINE
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| pubmed:month |
May
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| pubmed:issn |
1098-5336
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:volume |
77
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
3343-50
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| pubmed:dateRevised |
2011-11-1
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| pubmed:meshHeading |
pubmed-meshheading:21421786-Amino Acid Sequence,
pubmed-meshheading:21421786-Bacillus,
pubmed-meshheading:21421786-Coenzymes,
pubmed-meshheading:21421786-Enzyme Stability,
pubmed-meshheading:21421786-Escherichia coli,
pubmed-meshheading:21421786-Gene Expression,
pubmed-meshheading:21421786-Glucose,
pubmed-meshheading:21421786-Hydrogen-Ion Concentration,
pubmed-meshheading:21421786-Isomerases,
pubmed-meshheading:21421786-Kinetics,
pubmed-meshheading:21421786-Manganese,
pubmed-meshheading:21421786-Mannose,
pubmed-meshheading:21421786-Molecular Sequence Data,
pubmed-meshheading:21421786-Molecular Weight,
pubmed-meshheading:21421786-Pentoses,
pubmed-meshheading:21421786-Recombinant Proteins,
pubmed-meshheading:21421786-Substrate Specificity,
pubmed-meshheading:21421786-Temperature,
pubmed-meshheading:21421786-Thermus thermophilus,
pubmed-meshheading:21421786-Xylose
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| pubmed:year |
2011
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| pubmed:articleTitle |
Substrate specificity of the Bacillus licheniformis lyxose isomerase YdaE and its application in in vitro catalysis for bioproduction of lyxose and glucose by two-step isomerization.
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| pubmed:affiliation |
Bio-energy Research Institute, Chonnam National University, Gwangju 500-757, Republic of Korea.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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