Department of Life Sciences and Biotechnology, University of Ferrara, Via L. Borsari, 46, 44121 Ferrara, Italy.
Department of Biotechnology Engineering of the RRNN, Salesian Polytechnic University, Av. 12 de Octubre y Wilson, Quito 170109, Ecuador.
Int J Mol Sci. 2021 Mar 17;22(6):3066. doi: 10.3390/ijms22063066.
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.
布洛芬是一种非甾体抗炎药（NSAID），于 20 世纪 60 年代推出，广泛用作镇痛药、消炎药和解热药。在其酸形式下，21mg/L 的溶解度极大地限制了其生物利用度。由于药物产品的生物利用度在口服给药剂量设计中起着关键作用，因此本研究考察了布洛芬的酶酯化作为亲水化策略。这项工作提出了一种使用市售生物活性化合物的酸性官能团对高亲水分子进行共价攻击的酶策略。在正己烷/水两相体系中，使用廉价的生物催化剂猪胰腺脂肪酶（PPL）将布洛芬与山梨醇直接酯化，将疏水性差的药物布洛芬酯化，该酶被证明是有效生产 IBU-山梨醇酯的合适酶。本工作报道了酯化反应的优化。
