| pubmed-article:20640446 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20640446 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:20640446 | lifeskim:mentions | umls-concept:C1295886 | lld:lifeskim |
| pubmed-article:20640446 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:20640446 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:20640446 | lifeskim:mentions | umls-concept:C0024488 | lld:lifeskim |
| pubmed-article:20640446 | lifeskim:mentions | umls-concept:C0563532 | lld:lifeskim |
| pubmed-article:20640446 | lifeskim:mentions | umls-concept:C1521827 | lld:lifeskim |
| pubmed-article:20640446 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:20640446 | lifeskim:mentions | umls-concept:C0051154 | lld:lifeskim |
| pubmed-article:20640446 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:20640446 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:20640446 | pubmed:dateCreated | 2011-1-3 | lld:pubmed |
| pubmed-article:20640446 | pubmed:abstractText | The marine alginate lyase from Streptomyces sp. ALG-5, which specifically degrades poly-G block of alginate, was functionally expressed as a His-tagged form with an Escherichia coli expression system. The recombinant alginate lyase expressed with pColdI at 15 °C exhibited the highest alginate-degrading activity. The recombinant alginate lyase was efficiently immobilized onto two types of magnetic nanoparticles, superparamagnetic iron oxide nanoparticle, and hybrid magnetic silica nanoparticle, based on the affinity between His-tag and Ni(2+) that displayed on the surfaces of nanoparticles. An alginate oligosaccharide mixture consisting of dimer and trimer was prepared by the immobilized alginate lyase. The immobilized enzymes were re-used repeatedly more than 10 times after magnetic separation. | lld:pubmed |
| pubmed-article:20640446 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20640446 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20640446 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20640446 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20640446 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20640446 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20640446 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20640446 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20640446 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20640446 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:20640446 | pubmed:issn | 1615-7605 | lld:pubmed |
| pubmed-article:20640446 | pubmed:author | pubmed-author:ChoiSung... | lld:pubmed |
| pubmed-article:20640446 | pubmed:author | pubmed-author:LeeJae-HwaJH | lld:pubmed |
| pubmed-article:20640446 | pubmed:author | pubmed-author:LeeEun YeolEY | lld:pubmed |
| pubmed-article:20640446 | pubmed:author | pubmed-author:KimDong EunDE | lld:pubmed |
| pubmed-article:20640446 | pubmed:author | pubmed-author:LeeIn SuIS | lld:pubmed |
| pubmed-article:20640446 | pubmed:author | pubmed-author:KimHee SookHS | lld:pubmed |
| pubmed-article:20640446 | pubmed:author | pubmed-author:ShinJung... | lld:pubmed |
| pubmed-article:20640446 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20640446 | pubmed:volume | 34 | lld:pubmed |
| pubmed-article:20640446 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20640446 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20640446 | pubmed:pagination | 113-9 | lld:pubmed |
| pubmed-article:20640446 | pubmed:meshHeading | pubmed-meshheading:20640446... | lld:pubmed |
| pubmed-article:20640446 | pubmed:meshHeading | pubmed-meshheading:20640446... | lld:pubmed |
| pubmed-article:20640446 | pubmed:meshHeading | pubmed-meshheading:20640446... | lld:pubmed |
| pubmed-article:20640446 | pubmed:meshHeading | pubmed-meshheading:20640446... | lld:pubmed |
| pubmed-article:20640446 | pubmed:meshHeading | pubmed-meshheading:20640446... | lld:pubmed |
| pubmed-article:20640446 | pubmed:meshHeading | pubmed-meshheading:20640446... | lld:pubmed |
| pubmed-article:20640446 | pubmed:meshHeading | pubmed-meshheading:20640446... | lld:pubmed |
| pubmed-article:20640446 | pubmed:meshHeading | pubmed-meshheading:20640446... | lld:pubmed |
| pubmed-article:20640446 | pubmed:meshHeading | pubmed-meshheading:20640446... | lld:pubmed |
| pubmed-article:20640446 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:20640446 | pubmed:articleTitle | Heterologous expression of an alginate lyase from Streptomyces sp. ALG-5 in Escherichia coli and its use for preparation of the magnetic nanoparticle-immobilized enzymes. | lld:pubmed |
| pubmed-article:20640446 | pubmed:affiliation | Department of Chemical Engineering, Industrial Liaison Research Center, Kyung Hee University, Gyeonggi-do 446-701, Republic of Korea. | lld:pubmed |
| pubmed-article:20640446 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20640446 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
