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Updated: Dec 11, 2025

Synthesis of a Borylated Ibuprofen Derivative Through Suzuki Cross-Coupling and Alkene Boracarboxylation Reactions
Published on: November 30, 2022
A novel carboxylesterase from Acinetobacter sp. JNU9335 for efficient biosynthesis of Edoxaban precursor with high
Zhe Dou1, Guochao Xu1, Ye Ni1
1Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, PR China.
Abstract:
A novel carboxylesterase AcEst1 was identified from Acinetobacter sp. JNU9335 with high efficiency in the biosynthesis of chiral precursor of Edoxaban through kinetic resolution of methyl 3-cyclohexene-1-carboxylate (CHCM). Sequence analysis revealed AcEst1 belongs to family IV of esterolytic enzymes and exhibits <40% identities with known carboxylesterases. The optimum pH and temperature of recombinant AcEst1 are 8.0 and 40 °C. Substrate spectrum analysis indicated that AcEst1 prefers substrates with short acyl and alcohol groups. AcEst1 was highly active in the hydrolysis of CHCM with kcat of 1153 s-1 and displayed high substrate tolerance. As much as 2.0 M (280 g·L-1) CHCM could be enantioselectively hydrolyzed into (S)-CHCM by merely 0.08 g·L-1AcEst1 with ees of >99% (S) and substrate to catalyst ratio (S/C) of 3500 g·g-1. These results indicate that the novel AcEst1 is a promising biocatalyst in the synthesis of chiral carboxylic acids.
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