Biocatalytic approach for direct esterification of ibuprofen with sorbitol in biphasic media

Federico Zappaterra, Maria Elena Maldonado Rodriguez, Daniela Summa, Bruno Semeraro, Stefania Costa, Elena Tamburini

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

Ibuprofen is a nonsteroidal anti-inflammatory drug (NSAID) introduced in the 1960s and widely used as an analgesic, anti-inflammatory, and antipyretic. In its acid form, the solubility of 21 mg/L greatly limits its bioavailability. Since the bioavailability of a drug product plays a critical role in the design of oral administration dosage, this study investigated the enzymatic esterification of ibuprofen as a strategy for hydrophilization. This work proposes an enzymatic strategy for the covalent attack of highly hydrophilic molecules using acidic functions of commercially available bioactive compounds. The poorly water-soluble drug ibuprofen was esterified in a hexane/water biphasic system by direct esterification with sorbitol using the cheap biocatalyst porcine pancreas lipase (PPL), which demonstrated itself to be a suitable enzyme for the effective production of the IBU-sorbitol ester. This work reports the optimization of the esterification reaction.

Original languageEnglish
Article number3066
Pages (from-to)1-18
Number of pages18
JournalInternational Journal of Molecular Sciences
Volume22
Issue number6
DOIs
StatePublished - 2 Mar 2021

Bibliographical note

Publisher Copyright:
© 2021 by the authors. Licensee MDPI, Basel, Switzerland.

Keywords

  • Esterification
  • Ibuprofen
  • Porcine pancreas lipase
  • Prodrug
  • Sorbitol

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