Electrogravimetric Real-Time and in Situ Michaelis-Menten Enzimatic Kinetics: Progress Curve of Acetylcholinesterase Hydrolysis

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dc.contributor.authorBueno, Paulo Roberto [UNESP]
dc.contributor.authorWatanabe, Ailton M. [UNESP]
dc.contributor.authorFaria, Ronaldo C.
dc.contributor.authorSantos, Marcio L. [UNESP]
dc.contributor.authorRiccardi, Carla S. [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade Federal de São Carlos (UFSCar)
dc.date.accessioned2014-05-20T15:32:35Z
dc.date.available2014-05-20T15:32:35Z
dc.date.issued2010-12-16
dc.description.abstractA piezoelectric detection of enzyme-modified surface was performed under Michaelis-Menten presumptions of steady-state condition. The approach herein presented showed promise in the study of enzymatic kinetics by measuring the frequency changes associated with mass changes at the piezoelectric crystal surface. Likewise, real-time frequency shifts, that is, d Delta f/dt, indicated the rate of products formation from enzymatic reaction. In this paper, acetylcholinesterase was used as the enzymatic model and acetylcholine as substrate. The enzymatic rate has its maximum value for a short time during the kinetic reaction, for instance, during the first ten minutes of the reaction time scale. The values found for the kinetic constant rate and Michaelis-Menten constant were (1.4 +/- 0.8) 10(5) s(-1) and (5.2 +/- 3) 10(-4) M, respectively, in agreement with the values found in classical Michaelis-Menten kinetic experiments.en
dc.description.affiliationUniv Estadual Paulista, Inst Quim, BR-14800900 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Carlos (UFSCar), Dept Quim, BR-13560905 São Paulo, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Inst Quim, BR-14800900 São Paulo, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.format.extent16605-16610
dc.identifierhttp://dx.doi.org/10.1021/jp106274m
dc.identifier.citationJournal of Physical Chemistry B. Washington: Amer Chemical Soc, v. 114, n. 49, p. 16605-16610, 2010.
dc.identifier.doi10.1021/jp106274m
dc.identifier.issn1520-6106
dc.identifier.lattes0477045906733254
dc.identifier.orcid0000-0003-2827-0208
dc.identifier.urihttp://hdl.handle.net/11449/41452
dc.identifier.wosWOS:000284990700068
dc.language.isoeng
dc.publisherAmer Chemical Soc
dc.relation.ispartofJournal of Physical Chemistry B
dc.relation.ispartofjcr3.146
dc.relation.ispartofsjr1,331
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.titleElectrogravimetric Real-Time and in Situ Michaelis-Menten Enzimatic Kinetics: Progress Curve of Acetylcholinesterase Hydrolysisen
dc.typeResumo
dcterms.licensehttp://pubs.acs.org/page/copyright/journals/faqs.html
dcterms.rightsHolderAmer Chemical Soc
unesp.author.lattes0477045906733254[1]
unesp.author.lattes0173401604473200[5]
unesp.author.orcid0000-0003-2827-0208[1]
unesp.author.orcid0000-0003-2192-5312[5]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Química, Araraquarapt

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Artigos - Físico Química - IQ