Enantioselective extraction of unprotected amino acids coupled with racemization

Haofei Huang, Yingji Jin, Mukesh E. Shirbhate, Dayoung Kang, Misun Choi, Qian Chen, Youngmee Kim, Sung-Jin Kim, Il-Suk Byun, Ming Wang, Jean Bouffard (), Seong Kyu Kim () and Kwan Mook Kim ()
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Haofei Huang: Shandong University of Technology
Yingji Jin: Ewha Womans University
Mukesh E. Shirbhate: Ewha Womans University
Dayoung Kang: Ewha Womans University
Misun Choi: Ewha Womans University
Qian Chen: Ewha Womans University
Youngmee Kim: Ewha Womans University
Sung-Jin Kim: Ewha Womans University
Il-Suk Byun: R&D Center
Ming Wang: Shandong University of Technology
Jean Bouffard: Ewha Womans University
Seong Kyu Kim: Sungkyunkwan University
Kwan Mook Kim: Ewha Womans University

Nature Communications, 2021, vol. 12, issue 1, 1-7

Abstract: Abstract Scalable and economical methods for the production of optically pure amino acids, both natural and unnatural, are essential for their use as synthetic building blocks. Currently, enzymatic dynamic kinetic resolution (DKR) underpins some of the most effective processes. Here we report the development of enantioselective extraction coupled with racemization (EECR) for the chirality conversion of underivatized amino acids. In this process, the catalytic racemization of amino acids in a basic aqueous solution is coupled with the selective extraction of one enantiomer into an organic layer. Back-extraction from the organic layer to an acidic aqueous solution then completes the deracemization of the amino acid. The automation of the EECR process in a recycling flow reactor is also demonstrated. Continuous EECR is made possible by the sterically hindered chiral ketone extractant 5, which prevents the coextraction of the copper racemization catalyst because of its nonplanar geometry. Furthermore, the extractant 5 unexpectedly forms imines with amino acids faster and with greater enantioselectivity than less bulky derivatives, even though 5 cannot participate in intramolecular resonance-assisted hydrogen bonding. These features may allow EECR to challenge the preponderance of enzymatic DKR in the production of enantiomerically enriched amino acids.

Date: 2021
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DOI: 10.1038/s41467-020-20402-x

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