pubmed-article:21421786 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:21421786 | lifeskim:mentions | umls-concept:C0314875 | lld:lifeskim |
pubmed-article:21421786 | lifeskim:mentions | umls-concept:C0022202 | lld:lifeskim |
pubmed-article:21421786 | lifeskim:mentions | umls-concept:C0017725 | lld:lifeskim |
pubmed-article:21421786 | lifeskim:mentions | umls-concept:C0038592 | lld:lifeskim |
pubmed-article:21421786 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
pubmed-article:21421786 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
pubmed-article:21421786 | lifeskim:mentions | umls-concept:C0185125 | lld:lifeskim |
pubmed-article:21421786 | lifeskim:mentions | umls-concept:C0065419 | lld:lifeskim |
pubmed-article:21421786 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:21421786 | pubmed:dateCreated | 2011-5-12 | lld:pubmed |
pubmed-article:21421786 | 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. | lld:pubmed |
pubmed-article:21421786 | pubmed:language | eng | lld:pubmed |
pubmed-article:21421786 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21421786 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:21421786 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21421786 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21421786 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21421786 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21421786 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21421786 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21421786 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21421786 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21421786 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21421786 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:21421786 | pubmed:month | May | lld:pubmed |
pubmed-article:21421786 | pubmed:issn | 1098-5336 | lld:pubmed |
pubmed-article:21421786 | pubmed:author | pubmed-author:LeeSeong-Gene... | lld:pubmed |
pubmed-article:21421786 | pubmed:author | pubmed-author:WiSeung GonSG | lld:pubmed |
pubmed-article:21421786 | pubmed:author | pubmed-author:BaeHyeun-Jong... | lld:pubmed |
pubmed-article:21421786 | pubmed:author | pubmed-author:LeeDae-SeokDS | lld:pubmed |
pubmed-article:21421786 | pubmed:author | pubmed-author:PatelDarshan... | lld:pubmed |
pubmed-article:21421786 | pubmed:author | pubmed-author:SongYoun-hoYH | lld:pubmed |
pubmed-article:21421786 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:21421786 | pubmed:volume | 77 | lld:pubmed |
pubmed-article:21421786 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:21421786 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:21421786 | pubmed:pagination | 3343-50 | lld:pubmed |
pubmed-article:21421786 | pubmed:dateRevised | 2011-11-1 | lld:pubmed |
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pubmed-article:21421786 | pubmed:year | 2011 | lld:pubmed |
pubmed-article:21421786 | 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. | lld:pubmed |
pubmed-article:21421786 | pubmed:affiliation | Bio-energy Research Institute, Chonnam National University, Gwangju 500-757, Republic of Korea. | lld:pubmed |
pubmed-article:21421786 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:21421786 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |