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dc.contributor.authorCosta, Valentim Emilio Ubertipt_BR
dc.contributor.authorAmorim, Hermes Luis Neubauerpt_BR
dc.date.accessioned2013-07-03T01:42:36Zpt_BR
dc.date.issued1999pt_BR
dc.identifier.issn0100-4042pt_BR
dc.identifier.urihttp://hdl.handle.net/10183/72961pt_BR
dc.description.abstractIn organic synthesis, lipases are the most frequently used biocatalysts. They are efficient stereoselective catalysts in the kinetic resolution of a wide variety of chiral compounds. The discovery that enzymes possess catalytic activity in organic solvents has made it possible to address the question of reaction medium influence on enzymatic specificity. Perhaps the most exciting and significant development in this emerging area is the discovery that enzyme specificity, in particular enantioselectivity, can be affected by changing from one organic solvent to another. This article discusses the scope and possible mechanistic models of this phenomenon in hydrolases, specially lipases, as well as directions of future research in the area.en
dc.format.mimetypeapplication/pdfpt_BR
dc.language.isoporpt_BR
dc.relation.ispartofQuimica Nova. Sao Paulo, S.P. Vol. 22, n. 6 (nov./dez. 1999), p. 863-873pt_BR
dc.rightsOpen Accessen
dc.subjectSíntese orgânicapt_BR
dc.subjectLipase enantioselectivityen
dc.subjectSolventen
dc.subjectMechanistic modelsen
dc.titleO emprego de lipases como agentes de resolução cinética de enantiômeros em síntese orgânica : aspectos gerais sobre a influência do solventept_BR
dc.title.alternativeThe use of lipases as agents of kinetic resolution of enantiomers in organic synthesis : general aspects of solvent's influence en
dc.typeArtigo de periódicopt_BR
dc.identifier.nrb000247434pt_BR
dc.type.originNacionalpt_BR


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