pubmed-article:16384546 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16384546 | lifeskim:mentions | umls-concept:C0041484 | lld:lifeskim |
pubmed-article:16384546 | lifeskim:mentions | umls-concept:C0043491 | lld:lifeskim |
pubmed-article:16384546 | lifeskim:mentions | umls-concept:C0070570 | lld:lifeskim |
pubmed-article:16384546 | lifeskim:mentions | umls-concept:C0600364 | lld:lifeskim |
pubmed-article:16384546 | lifeskim:mentions | umls-concept:C1450054 | lld:lifeskim |
pubmed-article:16384546 | lifeskim:mentions | umls-concept:C1705938 | lld:lifeskim |
pubmed-article:16384546 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
pubmed-article:16384546 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:16384546 | pubmed:dateCreated | 2006-1-24 | lld:pubmed |
pubmed-article:16384546 | pubmed:abstractText | A mediator-free phenol biosensor was developed. The low-isoelectric point tyrosinase was adsorbed on the surface of high-isoelectric point ZnO nanoparticles (nano-ZnO) facilitated by the electrostatic interactions and then immobilized on the glassy carbon electrode via the film forming by chitosan. It was found that the nano-ZnO matrix provided an advantageous microenvironment in terms of its favorable isoelectric point for tyrosinase loading and the immobilized tyrosinase retaining its activity to a large extent. Moreover, there is no need to use any other electron mediators. Phenolic compounds were determined by the direct reduction of biocatalytically generated quinone species at -200mV (vs. saturated calomel electrode). The parameters of the fabrication process and the various experimental variables for the enzyme electrode were optimized. The resulting biosensor can reach 95% of steady-state current within 10s, and the sensitivity was as high as 182microAmmol(-1)L. The linear range for phenol determination was from 1.5x10(-7) to 6.5x10(-5)molL(-1) with a detection limit of 5.0x 10(-8)molL(-1) obtained at a signal/noise ratio of 3. In addition, the apparent Michaelis-Menten constant (K(m)(app)) and the stability of the enzyme electrode were estimated. The performance of the developed biosensor was compared with that of biosensors based on other immobilization matrices. | lld:pubmed |
pubmed-article:16384546 | pubmed:language | eng | lld:pubmed |
pubmed-article:16384546 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16384546 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16384546 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16384546 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16384546 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16384546 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16384546 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16384546 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16384546 | pubmed:month | Feb | lld:pubmed |
pubmed-article:16384546 | pubmed:issn | 0003-2697 | lld:pubmed |
pubmed-article:16384546 | pubmed:author | pubmed-author:Guo-LiShenS | lld:pubmed |
pubmed-article:16384546 | pubmed:author | pubmed-author:Ru-QinYuY | lld:pubmed |
pubmed-article:16384546 | pubmed:author | pubmed-author:LiuZhi-MinZM | lld:pubmed |
pubmed-article:16384546 | pubmed:author | pubmed-author:LiuYan-LiYL | lld:pubmed |
pubmed-article:16384546 | pubmed:author | pubmed-author:YangYun-HuiYH | lld:pubmed |
pubmed-article:16384546 | pubmed:author | pubmed-author:LiYin-FengYF | lld:pubmed |
pubmed-article:16384546 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16384546 | pubmed:day | 1 | lld:pubmed |
pubmed-article:16384546 | pubmed:volume | 349 | lld:pubmed |
pubmed-article:16384546 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16384546 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16384546 | pubmed:pagination | 33-40 | lld:pubmed |
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pubmed-article:16384546 | pubmed:year | 2006 | lld:pubmed |
pubmed-article:16384546 | pubmed:articleTitle | A mediator-free phenol biosensor based on immobilizing tyrosinase to ZnO nanoparticles. | lld:pubmed |
pubmed-article:16384546 | pubmed:affiliation | State Key Laboratory for Chemo/Biosensing and Chemometrics, College of Chemistry and Chemical Engineering, Hunan University, Changsha 410082, People's Republic of China. | lld:pubmed |
pubmed-article:16384546 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16384546 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |