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dc.contributor.author
Moyano, Fernando
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dc.contributor.author
Setien, Evangelina
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dc.contributor.author
Silber, Juana J.
dc.contributor.author
Correa, Nestor Mariano
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dc.date.available
2017-08-31T19:03:27Z
dc.date.issued
2013-06
dc.identifier.citation
Moyano, Fernando; Setien, Evangelina; Silber, Juana J.; Correa, Nestor Mariano; Enzymatic Hydrolysis of N‑Benzoyl‑L‑Tyrosine p‑Nitroanilide by α‑Chymotrypsin in DMSO-Water/AOT/n‑Heptane Reverse Micelles: a unique interfacial effect on the enzymatic activity; American Chemical Society; Langmuir; 29; 26; 6-2013; 8245-8254
dc.identifier.issn
0743-7463
dc.identifier.uri
http://hdl.handle.net/11336/23371
dc.description.abstract
The reverse micelle (RM) media are very good as nanoreactors because they can create a unique microenvironment for carrying out a variety of chemical and biochemical reactions. The aim of the present work is to determine the influence of different water-dimethyl sulfoxide (DMSO) mixtures encapsulated in 1,4-bis-2-ethylhexylsulfosuccinate (AOT)/n-heptane RMs on the enzymatic hydrolysis of N-benzoyl-L-tyrosine p-nitroanilide (Bz-Try-pNA) by α- chymotrypsin (α-CT). The reaction was first studied in homogeneous media at different DMSO-water mixture compositions and in DMSO-water/AOT/n-heptane RMs. The hydrolysis rates of Bz-Try-pNA catalyzed by α-CT were determined by UV−vis spectroscopy. The reaction follows the Michaelis-Menten mechanism and the kinetic parameters: kcat, KM, and kcat/KM were evaluated under different conditions. In this homogeneous media, DMSO plays an important role in the solubilization process of the peptide which is almost insoluble in water, but it has a tremendous impact on the inactivation of α-CT. It is shown that the enzyme dissolved in a 20% molar ratio of the DMSO-water mixture does not present enzymatic activity. Dynamic light scattering has been used to assess the formation of DMSO-water/AOT/heptane RMs at different DMSO compositions. The results also show that there is preferential solvation of the AOT RM interface by water molecules. To test the use of these RMs as nanoreactors, the kinetic parameters for the enzymatic reaction in these systems have been evaluated. The parameters were determined at fixed WS {WS = ([water] + [DMSO])/[AOT] = 20} at different DMSO-water compositions. The results show that the Michaelis−Menten mechanism is valid for α-CT in all the RM systems studied and that the reaction takes place at the RM interface. Surprisingly, it was observed that the enzyme encapsulated by the RMs show catalytic effects with similar kcat/KM values at any DMSO composition investigated, which evidence that DMSO molecules are localized far from the RM interface.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Chemical Society
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Reverse Micelles
dc.subject
Α-Chymotrypsin
dc.subject.classification
Otras Ciencias Químicas
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dc.subject.classification
Ciencias Químicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Enzymatic Hydrolysis of N‑Benzoyl‑L‑Tyrosine p‑Nitroanilide by α‑Chymotrypsin in DMSO-Water/AOT/n‑Heptane Reverse Micelles: a unique interfacial effect on the enzymatic activity
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-08-30T13:53:15Z
dc.journal.volume
29
dc.journal.number
26
dc.journal.pagination
8245-8254
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
Washington DC
dc.description.fil
Fil: Moyano, Fernando. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Setien, Evangelina. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Química; Argentina
dc.description.fil
Fil: Silber, Juana J.. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Química; Argentina
dc.description.fil
Fil: Correa, Nestor Mariano. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.journal.title
Langmuir
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1021/la401103q
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/abs/10.1021/la401103q
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