Revisiting <i>Jatropha curcas</i> Monomeric Esterase: A Dienelactone Hydrolase Compatible with the Electrostatic Catapult Model
<i>Jatropha curcas</i> 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 <i...
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2021-10-01
|
| Series: | Biomolecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2218-273X/11/10/1486 |
| _version_ | 1797515214388723712 |
|---|---|
| author | Marcos Gustavo Araujo Schwarz Deborah Antunes Gabriela Coelho Brêda Richard Hemmi Valente Denise Maria Guimarães Freire |
| author_facet | Marcos Gustavo Araujo Schwarz Deborah Antunes Gabriela Coelho Brêda Richard Hemmi Valente Denise Maria Guimarães Freire |
| author_sort | Marcos Gustavo Araujo Schwarz |
| collection | DOAJ |
| description | <i>Jatropha curcas</i> 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 <i>J. curcas</i> seed did not fit the electrostatic catapult model for esterases/lipases. We decided to reevaluate this <i>J. curcas</i> 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. |
| first_indexed | 2024-03-10T06:42:21Z |
| format | Article |
| id | doaj.art-572621690e56417687a821df25e4c3a1 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-10T06:42:21Z |
| publishDate | 2021-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-572621690e56417687a821df25e4c3a12023-11-22T17:34:19ZengMDPI AGBiomolecules2218-273X2021-10-011110148610.3390/biom11101486Revisiting <i>Jatropha curcas</i> Monomeric Esterase: A Dienelactone Hydrolase Compatible with the Electrostatic Catapult ModelMarcos Gustavo Araujo Schwarz0Deborah Antunes1Gabriela Coelho Brêda2Richard Hemmi Valente3Denise Maria Guimarães Freire4Laboratório de Genômica Funcional e Bioinformática, Instituto Oswaldo Cruz, Fiocruz, Rio de Janeiro 21040900, BrazilLaboratório de Genômica Funcional e Bioinformática, Instituto Oswaldo Cruz, Fiocruz, Rio de Janeiro 21040900, BrazilLaboratório de Microbiologia Molecular e Proteínas, Departamento de Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941909, BrazilLaboratório de Toxinologia, Instituto Oswaldo Cruz, Fiocruz, Rio de Janeiro 21040900, BrazilLaboratório de Biotecnologia Microbiana, Departamento de Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941909, Brazil<i>Jatropha curcas</i> 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 <i>J. curcas</i> seed did not fit the electrostatic catapult model for esterases/lipases. We decided to reevaluate this <i>J. curcas</i> 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.https://www.mdpi.com/2218-273X/11/10/1486<i>Jatropha curcas</i> L.seedesterasedienelactone hydrolase |
| spellingShingle | Marcos Gustavo Araujo Schwarz Deborah Antunes Gabriela Coelho Brêda Richard Hemmi Valente Denise Maria Guimarães Freire Revisiting <i>Jatropha curcas</i> Monomeric Esterase: A Dienelactone Hydrolase Compatible with the Electrostatic Catapult Model Biomolecules <i>Jatropha curcas</i> L. seed esterase dienelactone hydrolase |
| title | Revisiting <i>Jatropha curcas</i> Monomeric Esterase: A Dienelactone Hydrolase Compatible with the Electrostatic Catapult Model |
| title_full | Revisiting <i>Jatropha curcas</i> Monomeric Esterase: A Dienelactone Hydrolase Compatible with the Electrostatic Catapult Model |
| title_fullStr | Revisiting <i>Jatropha curcas</i> Monomeric Esterase: A Dienelactone Hydrolase Compatible with the Electrostatic Catapult Model |
| title_full_unstemmed | Revisiting <i>Jatropha curcas</i> Monomeric Esterase: A Dienelactone Hydrolase Compatible with the Electrostatic Catapult Model |
| title_short | Revisiting <i>Jatropha curcas</i> Monomeric Esterase: A Dienelactone Hydrolase Compatible with the Electrostatic Catapult Model |
| title_sort | revisiting i jatropha curcas i monomeric esterase a dienelactone hydrolase compatible with the electrostatic catapult model |
| topic | <i>Jatropha curcas</i> L. seed esterase dienelactone hydrolase |
| url | https://www.mdpi.com/2218-273X/11/10/1486 |
| work_keys_str_mv | AT marcosgustavoaraujoschwarz revisitingijatrophacurcasimonomericesteraseadienelactonehydrolasecompatiblewiththeelectrostaticcatapultmodel AT deborahantunes revisitingijatrophacurcasimonomericesteraseadienelactonehydrolasecompatiblewiththeelectrostaticcatapultmodel AT gabrielacoelhobreda revisitingijatrophacurcasimonomericesteraseadienelactonehydrolasecompatiblewiththeelectrostaticcatapultmodel AT richardhemmivalente revisitingijatrophacurcasimonomericesteraseadienelactonehydrolasecompatiblewiththeelectrostaticcatapultmodel AT denisemariaguimaraesfreire revisitingijatrophacurcasimonomericesteraseadienelactonehydrolasecompatiblewiththeelectrostaticcatapultmodel |