pubmed-article:18585147 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18585147 | lifeskim:mentions | umls-concept:C0016564 | lld:lifeskim |
pubmed-article:18585147 | lifeskim:mentions | umls-concept:C0027270 | lld:lifeskim |
pubmed-article:18585147 | lifeskim:mentions | umls-concept:C1511790 | lld:lifeskim |
pubmed-article:18585147 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
pubmed-article:18585147 | lifeskim:mentions | umls-concept:C0600364 | lld:lifeskim |
pubmed-article:18585147 | lifeskim:mentions | umls-concept:C0001861 | lld:lifeskim |
pubmed-article:18585147 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:18585147 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
pubmed-article:18585147 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:18585147 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
pubmed-article:18585147 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:18585147 | pubmed:dateCreated | 2008-6-30 | lld:pubmed |
pubmed-article:18585147 | pubmed:abstractText | An amperometric enzyme-based sensor-system for the direct detection of formaldehyde in air is under investigation. The biosensor is based on a native bacterial NAD(+)- and glutathione-independent formaldehyde dehydrogenase as biorecognition element. The enzyme was isolated from Hyphomicrobium zavarzinii strain ZV 580, grown on methylamine hydrochloride in a fed-batch process. The sensor depends on the enzymatic conversion of the analyte to formic acid. Released electrons are detected in an amperometric measurement at 0.2V vs. Ag/AgCl reference electrode by means of a redox-mediator. To optimize the sensing device, Ca(2+) and pyrroloquinoline quinone (PQQ) were added to the buffer solution as reconstitutional substances. At this stage, the sensor shows linear response in the tested ppm-range with a sensitivity of 0.39 microA/ppm. The signal is highly reproducible with respect to sensitivity and base line signal. Reproducibility of sensitivity is more than 90% within the same bacterial batch and even when enzyme of different bacterial batches is used. | lld:pubmed |
pubmed-article:18585147 | pubmed:language | eng | lld:pubmed |
pubmed-article:18585147 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18585147 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18585147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18585147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18585147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18585147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18585147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18585147 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18585147 | pubmed:month | May | lld:pubmed |
pubmed-article:18585147 | pubmed:issn | 1873-3573 | lld:pubmed |
pubmed-article:18585147 | pubmed:author | pubmed-author:HermannMM | lld:pubmed |
pubmed-article:18585147 | pubmed:author | pubmed-author:MoosRR | lld:pubmed |
pubmed-article:18585147 | pubmed:author | pubmed-author:FreitagRR | lld:pubmed |
pubmed-article:18585147 | pubmed:author | pubmed-author:JérômeVV | lld:pubmed |
pubmed-article:18585147 | pubmed:author | pubmed-author:HämmerliII | lld:pubmed |
pubmed-article:18585147 | pubmed:author | pubmed-author:AchmannSS | lld:pubmed |
pubmed-article:18585147 | pubmed:author | pubmed-author:HilbrigFF | lld:pubmed |
pubmed-article:18585147 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:18585147 | pubmed:day | 15 | lld:pubmed |
pubmed-article:18585147 | pubmed:volume | 75 | lld:pubmed |
pubmed-article:18585147 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18585147 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18585147 | pubmed:pagination | 786-91 | lld:pubmed |
pubmed-article:18585147 | pubmed:meshHeading | pubmed-meshheading:18585147... | lld:pubmed |
pubmed-article:18585147 | pubmed:meshHeading | pubmed-meshheading:18585147... | lld:pubmed |
pubmed-article:18585147 | pubmed:meshHeading | pubmed-meshheading:18585147... | lld:pubmed |
pubmed-article:18585147 | pubmed:meshHeading | pubmed-meshheading:18585147... | lld:pubmed |
pubmed-article:18585147 | pubmed:meshHeading | pubmed-meshheading:18585147... | lld:pubmed |
pubmed-article:18585147 | pubmed:meshHeading | pubmed-meshheading:18585147... | lld:pubmed |
pubmed-article:18585147 | pubmed:meshHeading | pubmed-meshheading:18585147... | lld:pubmed |
pubmed-article:18585147 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18585147 | pubmed:articleTitle | Direct detection of formaldehyde in air by a novel NAD+- and glutathione-independent formaldehyde dehydrogenase-based biosensor. | lld:pubmed |
pubmed-article:18585147 | pubmed:affiliation | Chair of Functional Materials, University of Bayreuth, 95440 Bayreuth, Germany. Sabine.Achmann@uni-bayreuth.de | lld:pubmed |
pubmed-article:18585147 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18585147 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18585147 | lld:pubmed |