Linked Life Data

17306226

Source:http://linkedlifedata.com/resource/pubmed/id/17306226

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2007-2-27
pubmed:abstractText
Immobilized proteins and enzymes were widely investigated in medical field as well as in food and environmental fields. In this paper, glucose oxidase (GOD) monolayer was covalently immobilized on the surface of gold nanoparticles (AuNPs) to fabricate bioconjugate complex. The citrate-stabilized AuNPs were first functionalized by a carboxyl-terminated alkanethiol and the terminal carboxyl groups were subsequently bonded with side-chain amino groups of protein surface through EDC/NHS coupling reaction. The enzyme activity assays of the obtained bioconjugates display an enhanced thermostability and similar pH-dependence behavior in contrast with that of free enzyme. Such GOD/AuNPs bioconjugates can be considered as a catalytic nanodevice to construct nanoreactor based on glucose oxidation reaction for biotechnological purpose.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
355
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
488-93
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Immobilization of glucose oxidase onto gold nanoparticles with enhanced thermostability.
pubmed:affiliation
Beijing National Laboratory for Molecular Sciences (BNLMS), International Joint Lab, CAS Key Lab of Colloid and Interface Science, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100080, PR China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't