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AutorSchwarz, Marcos Gustavo Araujo
AutorAntunes, Deborah
AutorBrêda, Gabriela Coelho
AutorValente, Richard Hemmi
AutorFreire, Denise Maria Guimarães
Fecha de acceso2021-11-09T18:54:38Z
Fecha de disponibilización2021-11-09T18:54:38Z
Fecha de publicación2021
ReferenciaSCHWARZ, Marcos Gustavo et al. Revisiting Jatropha curcas Monomeric Esterase: A Dienelactone Hydrolase Compatible with the Electrostatic Catapult Model. Biomolecules, v. 11, 1486, p. 1-20, 2021.pt_BR
ISSN2218-273Xpt_BR
URIhttps://www.arca.fiocruz.br/handle/icict/49755
Idiomaengpt_BR
EditorMDPIpt_BR
Derechos de autoropen access
Palabras clave en PortuguésJatropha curcas L.pt_BR
Palabras clave en PortuguésSementept_BR
Palabras clave en PortuguésEsterasept_BR
Palabras clave en PortuguésDienelactona hidrolasept_BR
TítuloRevisiting Jatropha curcas Monomeric Esterase: A Dienelactone Hydrolase Compatible with the Electrostatic Catapult Modelpt_BR
Tipo del documentoArticle
DOI10.3390/biom11101486
Resumen en InglésJatropha curcas contains seeds with a high oil content, suitable for biodiesel production. After oil extraction, the remaining mass can be a rich source of enzymes. However, data from the literature describing physicochemical characteristics for a monomeric esterase from the J. curcas seed did not fit the electrostatic catapult model for esterases/lipases. We decided to reevaluate this J. curcas esterase and extend its characterization to check this apparent discrepancy and gain insights into the enzyme’s potential as a biocatalyst. After anion exchange chromatography and two-dimensional gel electrophoresis, we identified the enzyme as belonging to the dienelactone hydrolase family, characterized by a cysteine as the nucleophile in the catalytic triad. The enzyme displayed a basic optimum hydrolysis pH of 9.0 and an acidic pI range, in contrast to literature data, making it well in line with the electrostatic catapult model. Furthermore, the enzyme showed low hydrolysis activity in an organic solvent-containing medium (isopropanol, acetonitrile, and ethanol), which reverted when recovering in an aqueous reaction mixture. This enzyme can be a valuable tool for hydrolysis reactions of short-chain esters, useful for pharmaceutical intermediates synthesis, due to both its high hydrolytic rate in basic pH and its stability in an organic solvent.pt_BR
AfiliaciónFundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Genômica Funcional e Bioinformática. Rio de Janeiro, RJ, Brasil.pt_BR
AfiliaciónFundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Genômica Funcional e Bioinformática. Rio de Janeiro, RJ, Brasil.pt_BR
AfiliaciónUniversidade Federal do Rio de Janeiro. Instituto de Química. Departamento de Bioquímica. Laboratório de Microbiologia Molecular e Proteínas. Rio de Janeiro, RJ, Brasil.pt_BR
AfiliaciónFundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ, Brasilpt_BR
AfiliaciónUniversidade Federal do Rio de Janeiro. Instituto de Química. Departamento de Bioquímica. Laboratório de Biotecnologia Microbiana. Rio de Janeiro, RJ, Brasil .pt_BR
Palavras clave en InglêsJatropha curcas L.pt_BR
Palavras clave en InglêsSeedpt_BR
Palavras clave en InglêsEsterasept_BR
Palavras clave en InglêsDienelactone hydrolasept_BR


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